Abstract. The use of recombinant peptides based upon the repeated amino acid sequences of Plasmodium has been proposed for malaria vaccines. By reducing homologies of such peptide vaccines to host proteins, the possibility of autoimmune complications may be reduced, and the effective immune response may be enhanced. The Wilbur and Lipman Wordsearch algorithm was used to identify homologous amino acid sequences between tandemly repeated Plasmodium amino acid sequences and the human and human viral sequences compiled in the National Biomedical Research Foundation database. Six published repetitive immunogenic amino acid sequences from the circumsporozoite (CS) antigen, ring-infected erythrocyte surface antigen (RESA), soluble (S) antigen, and falciparum interspersed repetitive antigen (FIRA) of P. falciparum, and the CS protein of P. vivax, were analyzed by computer. Matches of at least 4 amino acids were found for all sequences. In the database, 29 matches were found for human proteins and 26 matches
Chang, E., et al. N-Terminal Amino Acid Sequence Determination of Proteins by N-Terminal Dimethyl Labeling: Pitfalls and Advantages When Compared with Edman Degradation Sequence Analysis. Journal of Biomolecular Technology. 27(2). 07/03/2016.. ...
The complete amino acid sequence of bovine S antigen (48-kDa protein) has been determined by cDNA and partial amino acid sequencing. A 1623-base-pair (bp) cDNA contains an open reading frame coding for a protein of 404 amino acids (45,275 Da). Tryptic peptides and cyanogen bromide peptides of native bovine S antigen were purified and partially sequenced. All of these peptides were accounted for in the long open reading frame. Searching of the National Biomedical Research Foundation data bank revealed no extensive sequence homology between S antigen and other proteins. However, there are local regions of sequence similarity with alpha transducin, including the sites subject to ADP-ribosylation by Bordetella pertussis and cholera toxins and the phosphoryl binding-sites. Secondary structure prediction and circular dichroic spectroscopy show that S antigen is composed predominantly of beta-sheet conformation. Acid-catalyzed methanolysis suggests the presence of low levels of carbohydrate in the ...
Protein primary structure is the linear sequence of amino acids in a peptide or protein. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory[citation needed]. Protein primary structures can be directly sequenced, or inferred from DNA sequences. Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding along it. In biological systems, proteins are produced during translation by a cells ribosomes. Some organisms can also make short peptides by non-ribosomal peptide synthesis, which often use amino acids other than the standard 20, and may be cyclised, modified and cross-linked. Peptides can be synthesised chemically via a range of laboratory methods. Chemical methods typically synthesise peptides in the opposite order to ...
37 CFR 1.822(c)(5) provides that nucleotide sequences shall only be represented by a single strand, in the 5′ to 3′ direction, from left to right. That is, double stranded nucleotides shall not be represented in the sequence listing. A double stranded nucleotide may be represented as two single stranded nucleotides, and any relationship between the two may be shown in the drawings. The procedures for presenting and numbering amino acid sequences are set forth in 37 CFR 1.822(d). Two alternatives are presented for numbering amino acid sequences. Amino acid sequences may be numbered with respect to the identification of the first amino acid of the first mature protein or with respect to the first amino acid appearing at the amino terminal. The numbering procedure for nucleotides is set forth in 37 CFR 1.822(c)(6). Sequences that are circular in configuration are intended to be encompassed by these rules, and the numbering procedures described above remain applicable with the exception that the ...
Genetic susceptibility to autoimmunity is frequently associated with specific MHC alleles. Diabetogenic MHC class II molecules, such as human HLA-DQ8 and mouse I-Ag7, typically have a small, uncharged amino acid residue at position 57 of their β chain (β57); this results in the absence of a salt bridge between β57 and Argα76, which is adjacent to the P9 pocket of the peptide-binding groove. However, the influence of Argα76 on the selection of the TCR repertoire remains unknown, particularly when the MHC molecule binds a peptide with a neutral amino acid residue at position P9. Here, we have shown that diabetogenic MHC class II molecules bound to a peptide with a neutral P9 residue primarily selected and expanded cells expressing TCRs bearing a negatively charged residue in the first segment of their complementarity determining region 3β. The crystal structure of one such TCR in complex with I-Ag7 bound to a peptide containing a neutral P9 residue revealed that a network of favorable ...
The invention provides a method for determining an amino acid sequence motif for a phosphorylation site of a protein kinase. In the method of the invention, a protein kinase is contacted with an oriented degenerate peptide library, peptides within the library which are substrates for the kinase are converted to phosphopeptides and the phosphopeptides are separated from non-phosphorylated peptides. The isolated phosphopeptides are sequenced and an amino acid sequence motif for the phosphorylation site is determined based upon the relative abundance of different amino acids residues at each degenerate position. The invention also provides peptide substrates for protein kinase A, cell cycle control kinases, src family kinases, the EGF receptor and p92.sup.c-fps/fes based upon amino acid sequence motifs for the phosphorylation sites of these kinases.
Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɪnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino ...
TY - JOUR. T1 - The hormonal control of glycogen metabolism. T2 - The amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1. AU - Cohen, Philip. AU - Rylatt, Dennis B.. AU - Nimmo, Gillian A.. PY - 1977/4/15. Y1 - 1977/4/15. UR - http://www.scopus.com/inward/record.url?scp=0017407844&partnerID=8YFLogxK. U2 - 10.1016/0014-5793(77)80147-6. DO - 10.1016/0014-5793(77)80147-6. M3 - Article. C2 - 193727. AN - SCOPUS:0017407844. VL - 76. SP - 182. EP - 186. JO - FEBS Letters. JF - FEBS Letters. SN - 0014-5793. IS - 2. ER - ...
TY - JOUR. T1 - Deduced primary structure of rat tryptophan-2,3-dioxygenase. AU - Maezono, Katsumi. AU - Tashiro, Kosuke. AU - Nakamura, Toshikazu. PY - 1990/7/16. Y1 - 1990/7/16. N2 - The complete amino acid sequence of the tryptophan 2, 3-dioxygenase (TO) of rat liver was determined from the nucleotide sequence of a full length TO cDNA isolated from a rat liver cDNA library and determined its primary structure. TO was encoded in a mRNA of about 1.7 kb containing an open reading frame of 1218 bp. According to the deduced amino acid sequence, the monomeric polypeptide of TO consisted of 406 amino acid residues with a calculated molecular weight of 47,796 daltons. It has twelve histidine residues around its hydrophobic region, which has homology with some heme proteins and oxygenase, suggesting that this hydrophobic region might to be the core of TO for the activity.. AB - The complete amino acid sequence of the tryptophan 2, 3-dioxygenase (TO) of rat liver was determined from the nucleotide ...
The amino acid sequences of the CT and TMD of NA are highly and moderately conserved, respectively, among the influenza A viruses. Yet the specific function and role of these amino acid sequences in virus biology remain unknown. Results presented in this report show that the specific amino acid residues are not absolutely required for the influenza virus life cycle, since either the complete or part of the NA TMD or CT can be replaced and modified, yet infectious viruses can be rescued and propagated. On the other hand, our data show that specific amino acids in some regions of the TMD and CT as well as a foreign TMD have a profound influence on virus biology, causing reduction in growth during multiple cycles of infection. Reduced yield of NA mutants can be attributed to decreased enzyme activity in the virion and a defect in budding at the cell surface.. Mutations in the TMD and CT of NA can affect protein expression, maturation, transport, incorporation into virions, and enzyme activity and ...
...COLLEGE STATION - Functional amino acids play a critical role in the d...In a journal article appearing in the American Society for Nutrition (... We need to move forward and capitalize on the potential of functional...A functional amino acid is an amino acid that can regulate key metabol...,AgriLife,scientist:,Functional,amino,acids,regulate,key,metabolic,pathways,biological,biology news articles,biology news today,latest biology news,current biology news,biology newsletters
The CLV3/ESR-RELATED (CLE) gene family encodes small secreted peptides (SSPs) and plays vital roles in plant growth and development by promoting cell-to-cell communication. The prediction and classification of CLE genes is challenging because of their low sequence similarity. We developed a machine learning-aided method for predicting CLE genes by using a CLE motif-specific residual score matrix and a novel clustering method based on the Euclidean distance of 12 amino acid residues from the CLE motif in a site-weight dependent manner. In total, 2156 CLE candidates-including 627 novel candidates-were predicted from 69 plant species. The results from our CLE motif-based clustering are consistent with previous reports using the entire pre-propeptide. Characterization of CLE candidates provided systematic statistics on protein lengths, signal peptides, relative motif positions, amino acid compositions of different parts of the CLE precursor proteins, and decisive factors of CLE prediction. The approach
BACKGROUND: There is an increasing need to develop bioinformatic tools to organise and analyse the rapidly growing amount of nucleotide and amino acid sequence data in organisms ranging from viruses to eukaryotes. FINDING: A simple sequence editor (SSE) was developed to create an integrated environment where sequences can be aligned, annotated, classified and directly analysed by a number of built-in bioinformatic programs. SSE incorporates a sequence editor for the creation of sequence alignments, a process assisted by integrated CLUSTAL/MUSCLE alignment programs and automated removal of indels. Sequences can be fully annotated and classified into groups and annotated of sequences and sequence groups and access to analytical programs that analyse diversity, recombination and RNA secondary structure. Methods for analysing sequence diversity include measures of divergence and evolutionary distances, identity plots to detect regions of nucleotide or amino acid homology, reconstruction of sequence changes,
The GLI oncogene, discovered by virtue of its amplification in human tumors, encodes a sequence-specific DNA-binding protein containing five zinc fingers. We have now characterized one member of a family of GLI-related zinc finger genes. A previously identified fragment of GLI3 genomic DNA was used to localize GLI3 to chromosome 7p13 and to isolate cDNA clones. Sequence analysis of these clones and identification of the GLI3 protein by using polyclonal antisera demonstrated that GLI3 encodes a protein of 1,596 amino acids and an apparent molecular mass of 190 kilodaltons. Amino acid sequence comparison with GLI demonstrated seven regions of similarity (53 to 88% identity), with the zinc fingers representing the most similar region. Furthermore, when produced in vitro, the GLI3 protein bound specifically to genomic DNA fragments containing GLI-binding sites. Amino acid sequence comparison with the product of another member of the GLI family, the Drosophila segment polarity gene cubitus ...
Ubiquitin is a 76-residue protein highly conserved among eukaryotes. Conjugation of ubiquitin to intracellular proteins mediates their selective degradation in vivo. We describe a family of four ubiquitin-coding loci in the yeast Saccharomyces cerevisiae. UB11, UB12 and UB13 encode hybrid proteins in which ubiquitin is fused to unrelated (tail) amino acid sequences. The ubiquitin coding elements of UB11 and UB12 are interrupted at identical positions by non-homologous introns. UB11 and UB12 encode identical 52-residue tails, whereas UB13 encodes a different 76-residue tail. The tail amino acid sequences are highly conserved between yeast and mammals. Each tail contains a putative metal-binding, nucleic acid-binding domain of the form Cys-X2-4-Cys-X2-15-Cys-X2-4-Cys, suggesting that these proteins may function by binding to DNA. The fourth gene, UB14, encodes a polyubiquitin precursor protein containing five ubiquitin repeats in a head-to-tail, spacerless arrangement. All four ubiquitin genes ...
The primary structure of porcine brain beta-tubulin was determined by automated and manual Edman degradation of six sets of overlapping peptides. The protein consists of 445 amino acid residues and has a minimum of six positions that are heterogeneous, indicating at least two beta-tubulins in porcine brain. Comparison of the optimally aligned sequences of alpha-tubulin and beta-tubulin indicates that 41% of their primary structures are identical. A region rich in glycyl residues is similar both in sequence and predicted secondary structure to the phosphate binding loop of several nucleotide binding enzymes. beta-Tubulin contains a highly acidic COOH-terminal region that resembles the NH2-terminus of troponin T.. ...
A method is provided for isolating and identifying a recombinant clone having a DNA segment therein coding for at least one desired heterologous polypeptide, at least a short amino acid sequence of which is known, by effecting cDNA synthesis on a mixture of mRNAs containing the mRNA coding for the desired polypeptide, isolating the resultant cDNA mixture, inserting the resultant cDNA into recombinant cloning vehicles, transforming hosts with the vehicles, separating the transformants and isolating and identifying a recombinant clone containing a DNA segment which is homologous over at least a portion thereof to at least one oligonucleotide probe specific for the DNA segment; wherein the probe is an extension of the nucleotide sequence of an oligonucleotide primer having a nucleotide sequence complementary to a region of the target mRNA coding for a portion of the known amino acid sequence, and is complementary to a longer region of the target mRNA coding for a longer portion of the known amino acid
A method is provided for isolating and identifying a recombinant clone having a DNA segment therein coding for at least one desired heterologous polypeptide, at least a short amino acid sequence of which is known, by effecting cDNA synthesis on a mixture of mRNAs containing the mRNA coding for the desired polypeptide, isolating the resultant cDNA mixture, inserting the resultant cDNA into recombinant cloning vehicles, transforming hosts with the vehicles, separating the transformants and isolating and identifying a recombinant clone containing a DNA segment which is homologous over at least a portion thereof to at least one oligonucleotide probe specific for the DNA segment; wherein the probe is an extension of the nucleotide sequence of an oligonucleotide primer having a nucleotide sequence complementary to a region of the target mRNA coding for a portion of the known amino acid sequence, and is complementary to a longer region of the target mRNA coding for a longer portion of the known amino acid
TY - JOUR. T1 - Design of amino acid sequences to fold into C-alpha model proteins. AU - Amatori, Andrea. AU - Tiana, Guido. AU - Sutto, L.. AU - Ferkinghoff-Borg, Jesper. AU - Trovato, Antonio. AU - Broglia, Richardo A.. PY - 2005. Y1 - 2005. N2 - In order to extend the results obtained with minimal lattice models to more realistic systems, we study a model where proteins are described as a chain of 20 kinds of structureless amino acids moving in a continuum space and interacting through a contact potential controlled by a 2020 quenched random matrix. The goal of the present work is to design and characterize amino acid sequences folding to the SH3 conformation, a 60-residue recognition domain common to many regulatory proteins. We show that a number of sequences can fold, starting from a random conformation, to within a distance root-mean-square deviation between 2.6 and 4.0 Å from the native state. Good folders are those sequences displaying in the native conformation an energy lower than a ...
The amino acid sequences of 301 glycosyl hydrolases and related enzymes have been compared. A total of 291 sequences corresponding to 39 EC entries could be classified into 35 families. Only ten sequences (less than 5% of the sample) could not be assigned to any family. With the sequences available for this analysis, 18 families were found to be monospecific (containing only one EC number) and 17 were found to be polyspecific (containing at least two EC numbers). Implications on the folding characteristics and mechanism of action of these enzymes and on the evolution of carbohydrate metabolism are discussed. With the steady increase in sequence and structural data, it is suggested that the enzyme classification system should perhaps be revised. ...
The supernumerary subunit g is found in all mitochondrial ATP synthases. Most of the conserved amino acid residues are present in the membrane C-terminal part of the protein that contains a dimerization motif GXXXG. In yeast, alteration of this motif leads to the loss of subunit g and of supramolecular structures of the ATP synthase with concomitant appearance of anomalous mitochondrial morphologies. Disulfide bond formation involving an engineered cysteine in position 109 of subunit g and the endogenous cysteine 28 of subunit e promoted g + g, e + g, and e + e adducts, thus revealing the proximity in the mitochondrial membrane of several subunits e and g. Disulfide bond formation between two subunits g in mitochondria increased the stability of an oligomeric structure of the ATP synthase in digitonin extracts. These data suggest the participation of the dimerization motif of subunit g in the formation of supramolecular structures and is in favor of the existence of ATP synthase associations, in ...
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1993) The download the paraphrase of shem nh vii1 nag hammadi and manichaean lifetime equations through a internal detail into a right story-layered Africville at the electrical arrangement then in guy. 1978) In: Atlas of Protein Sequence and Structure, Suppl. 2 National Biomedical Research Foundation, Washington, DC.
The detection of HIV-1 p24 antigen in diagnostic tests relies on antibodies binding to conserved areas of the protein to cover the full range of HIV-1 subtypes. Using a panel of 43 different virus-like particles (VLPs) expressing Gag from clinical HIV-1 isolates, we previously found that some highly sensitive tests completely failed to detect p24 of certain VLPs, seemingly unrelated to their subtype. Here we aimed to investigate the reason for this failure, hypothesising that it might be due to single amino acid variations in conserved epitopes. Using amino acid alignment, we identified single amino acid variations at position 16 or 170 of p24, unique to those VLPs that failed to be detected in certain diagnostic tests. Through DNA-mutagenesis, these amino acids were changed to ones more commonly found at these positions. The impact of these changes on p24 detection was tested in commercial diagnostic tests as well as by Western Blot and ELISA, using epitope-specific antibodies. Changing positions 16 or
The observed gene overlays in the viruses ФX174 and SV40 show a surprising economy of information storage; two different amino acid sequences are read in different frames from the same stretch of DNA.
To determine the degree of similarity between pituitary and lymphocyte proopiomelanocortin, the lymphocyte mRNA was reverse transcribed, cloned, and sequenced. Murine lymphocyte mRNA was first purified by oligo(dT)-cellulose affinity chromatography and was reverse transcribed by using a selective 3′ antisense oligonucleotide primer directed at the boundary between the translated/nontranslated region on the 3′ end of exon 3. This cDNA was then amplified in a polymerase chain reaction with selective primers containing Sal I and Kpn I restriction endonuclease sites. Amplified cDNA was then directionally ligated into M13mp18 and M13mp19 bacteriophage and was sequenced. The nucleotide sequence encoding this peptide was identical to that of mouse pituitary corticotropin (ACTH). Elevated levels of lymphocyte immunoreactive ACTH were then induced with bacterial lipopolysaccharide and the peptide(s) was purified by antibody affinity chromatography and reverse-phase high-performance liquid ...
Amino acid sequence in DENV2 NS2B/NS3 protease. The residues marked in bold are part of NS2B amino acid sequence. The residues marked in underline are His-tag.
A standard technique to confirm the amino acid sequence of a molecule, Peptide Mapping Analysis uses multiple enzyme digest strategy to break apart a protein into smaller peptide fragments which are subsequently analysed on the mass spectrometer.. Peptide fragments digested with different enzymes will highly likely provide overlapping amino acid sequence data, allowing for the accurate determination and confirmation of the amino acid sequence of the full length of a target protein molecule.. An added value of Peptide Mapping Analysis is that modifications such as C-terminal truncations and/or N-terminal modifications may also be detected.. For more information please email [email protected] ...
Genomes and Genes, Research Topics, Scientific Experts, Species, Locale, Publications about Experts and Doctors on amino acid sequence in San Diego, California, United States
DNA damage can result in a variety of mutations, including point mutations, frameshift mutations, and chromosomal mutations. Point mutations include changes in DNA sequence due to substitution of one base for another during DNA replication. For example, the DNA sequence AATTCGCATTG could be replicated as AACTCGCCTTG. Changes in DNA sequence may or may not result in changes in amino acid sequence when the mutated DNA is used to code for protein. When DNA is translated into proteins, every three nucleotide bases (a codon) code for one amino acid. However, many amino acids are coded for by more than one codon. Thus, if a mutation occurs such that the mutated sequence codes for the same amino acid sequence as the old sequence, this is called a silent mutation. In evolutionary terms, this is also referred to as a neutral mutation. Silent (or neutral) mutations may also occur if there is a change in the amino acid sequence, but this does not alter the structure of the protein. However, if a point ...
An increasing number of proteins with weak sequence similarity have been found to assume similar three-dimensional fold and often have similar or related biochemical or biophysical functions. We propose a method for detecting the fold similarity between two proteins with low sequence similarity based on their amino acid properties alone. The method, the proximity correlation matrix (PCM) method, is built on the observation that the physical properties of neighboring amino acid residues in sequence at structurally equivalent positions of two proteins of similar fold are often correlated even when amino acid sequences are different. The hydrophobicity is shown to be the most strongly correlated property for all protein fold classes. The PCM method was tested on 420 proteins belonging to 64 different known folds, each having at least three proteins with little sequence similarity. The method was able to detect fold similarities for 40% of the 420 sequences. Compared with sequence comparison and ...
The results above define the location of the cleavage site in QSOX1A as occurring between the peptide sequence used to raise the anti-QSOX1A antibody and the TM domain (Figure 5A). To identify potential proteases responsible for the cleavage of QSOX1A, we first searched the UniProt database [26] for all proteases that are known to be present within the human ER and Golgi apparatus (Supplementary Table S1 at http://www.biochemj.org/bj/454/bj4540181add.htm). The resulting list of proteases was analysed manually with regard to their substrate specificities and consensus cleavage patterns. Three of the PPCs (proprotein convertases), PCSK3, PCSK6 and PCSK7, particularly stood out as they cleave at dibasic motifs, two of which are present in the QSOX1A amino acid sequence. The QSOX1A amino acid sequence also was analysed for potential cleavage sites using the ProP 1.0 Server [27]. Two of the predicted PPC cleavage sites are present in the region of interest with cleavage occurring C-terminally of ...
SEC72 encodes the 23-kD subunit of the Sec63p complex, an integral ER membrane protein complex that is required for translocation of presecretory proteins into the ER of Saccharomyces cerevisiae. DNA sequence analysis of SEC72 predicts a 21.6-kD protein with neither a signal peptide nor any transmembrane domains. Antibodies directed against a carboxyl-terminal peptide of Sec72p were used to confirm the membrane location of the protein. SEC72 is not essential for yeast cell growth, although an sec72 null mutant accumulates a subset of secretory precursors in vivo. Experiments using signal peptide chimeric proteins demonstrate that the sec72 translocation defect is associated with the signal peptide rather than with the mature region of the secretory precursor. ...
SEC72 encodes the 23-kD subunit of the Sec63p complex, an integral ER membrane protein complex that is required for translocation of presecretory proteins into the ER of Saccharomyces cerevisiae. DNA sequence analysis of SEC72 predicts a 21.6-kD protein with neither a signal peptide nor any transmembrane domains. Antibodies directed against a carboxyl-terminal peptide of Sec72p were used to confirm the membrane location of the protein. SEC72 is not essential for yeast cell growth, although an sec72 null mutant accumulates a subset of secretory precursors in vivo. Experiments using signal peptide chimeric proteins demonstrate that the sec72 translocation defect is associated with the signal peptide rather than with the mature region of the secretory precursor. ...
TY - JOUR. T1 - Insulin regulation of a novel WD-40 repeat protein in adipocytes. AU - Rodgers, B. D.. AU - Levine, M. A.. AU - Bernier, M.. AU - Montrose-Rafizadeh, C.. PY - 2001. Y1 - 2001. N2 - A 400 bp PCR product generated with degenerate primers derived from the glucagon-like peptide-1 receptor was used to screen a rat skeletal muscle cDNA library. The predicted amino acid sequence of the 978 bp open reading frame has a predicted Mr of 35 804, an estimated isoelectric point (pI) of 5.31 and contains seven WD-40 repeats, which are common to G-protein beta subunits (Gβ). Although chemically and structurally similar to Gβ subunits, the predicted amino acid sequence, when compared with the previously cloned Gβ isoforms, was found to be only 31-41% similar and thus was named Gβ-like (GβL, Gable). Western blotting of whole-cell lysates and immunoprecipitates of membrane and cytosolic fractions of HEK 293 cells stably overexpressing a carboxy-terminal His-tagged GβL indicates that the ...
A polynucleotide sequence for the mouse ortholog of human zalphal 1 has been identified and is shown in SEQ ID NO:84 and the corresponding amino acid sequence shown in jEQ ID NO: 85. AnalYsis of the mouse zalphal 1 polypeptide encoded by the DNA\ sequence of SEQ ID N0(84)revealed an open reading frame encodmg 529 amino acids (SEQ ID NO:85) comprising a predicted secretory signal peptide of 19 amino acid residues (residue 1 (Met) to residue 19 (Ser) of SEQ ID NO:85), and a mature polypeptide of 510 amino acids (residue 20 (Cys) to residue 529 (Ser) of SEQ ID N0:2). In addition to the WSXWS motif (SEQ ID N0:3) corresponding to residues 214 to 218 of SEQ ID N0:85, the receptor comprises a cytokine-binding domain of approximately 200 amino acid residues (residues 20 (Cys) to 237 (His) of SEQ ID N0:85); a domam linker (residues 120 (Pro) to 123 (Pro) of SEQ ID NO:85); a penultimate strand region (residues 192 (Lys) to 202 (Ala) of SEQ ID NO:85); a transmembrane domain (residues 238 (Met) to 254 (Leu) ...
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Adducin is a membrane-skeletal protein which is a candidate to promote assembly of a spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. The complete sequence of both subunits of human adducin, alpha (737 amino acids), and beta (726 amino acids) has been deduced by analysis of the cDNAs. The two subunits have strikingly conserved amino acid sequences with 49% identity and 66% similarity, suggesting evolution by gene duplication. Each adducin subunit has three distinct domains: a 39-kD NH2-terminal globular protease-resistant domain, connected by a 9-kD domain to a 33-kD COOH-terminal protease-sensitive tail comprised almost entirely of hydrophilic amino acids. The tail is responsible for the high frictional ratio of adducin noted previously, and was visualized by EM. The head domains of both adducin subunits exhibit a limited sequence similarity with the NH2-terminal actin-binding motif present in members of the spectrin superfamily and actin gelation ...
Maloy W.L.; Nathenson S.G.; Coligan J.E., 1981: Primary structure of murine major histo compatibility complex allo antigens amino acid sequence of the amino terminal 98 residues of the h 2d b glyco protein
The glycoprotein encoded by this gene is a cell surface antigen that is expressed in greater than 95% of human colon cancers. The open reading frame encodes a 319-amino acid polypeptide having a putative secretory signal sequence and 3 potential glycosylation sites. The predicted mature protein has a 213-amino acid extracellular region, a single transmembrane domain, and a 62-amino acid intracellular tail. The sequence of the extracellular region contains 2 domains characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily. [provided by RefSeq, Jul 2008 ...
The Cycle 1 results indicate that the N-terminal amino acid residue is D (aspartic acid). The Cycle 2 results indicate that the second amino acid group from the N-terminal is V (valine). Analysis to the 21st residue reveals the sequence from the N-terminal to be: Asp-Val-Val-Met-Thr-Gln-Thr-Pro-Leu-Thr-Leu-Ser-Val-Thr-Ile-Gly-Gln-Pro-Ala-Ser-Ile.. ...
TY - JOUR. T1 - The amino acid sequences of the phosphorylated sites in troponin-I from rabbit skeletal muscle. AU - Huang, T. S.. AU - Bylund, D. B.. AU - Stull, J. T.. AU - Krebs, E. G.. PY - 1974/6/15. Y1 - 1974/6/15. UR - http://www.scopus.com/inward/record.url?scp=0016165471&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0016165471&partnerID=8YFLogxK. U2 - 10.1016/0014-5793(74)80738-6. DO - 10.1016/0014-5793(74)80738-6. M3 - Article. C2 - 4369265. AN - SCOPUS:0016165471. VL - 42. SP - 249. EP - 252. JO - FEBS Letters. JF - FEBS Letters. SN - 0014-5793. IS - 3. ER - ...
Fig. 4 shows the amino acid sequences of the predicted proteins of AtFpg-1, -1a, -2, -3, and -4. Exons 1, 2, 3, 5, 6, and 7 were entirely conserved in all the Arabidopsis cDNA clones. The polypeptide chains encoded by exons 1, 5, 6,and 7 represent the major conserved regions between Arabidopsis and bacterial FPGs , showing between 29 and 54% identity between Arabidopsis and E. coli amino acid sequences. The N-terminal sequence of exon 1 and the lysine of exon 5 (K155) of E. coli FPG have been associated with the active site. The predicted amino acid sequence coded by exon 1 shows a surprising relationship to a sequence from DNA photolyase, another DNA repair enzyme but one quite unrelated to FPG (Fig. 5). If this relates to DNA binding, it might explain how AtFPG-2, which lacks the C-terminal DNA-binding region present in AtFPG-1 (or the zinc-finger of E. coli FPG) might have the DNA cleavage activities measured by Gao and Murphy (Photochem. Photobiol., in press). The optional exons are exon 4 ...
We have cloned the cDNA encoding a murine GDNF inducible transcription factor designated mGIF. It is homolgous to two human genes, TIEG (Subramaniam et al., 1995) and EGR-α (Blok et al., 1995). TIEG was cloned from fetal osteoblastic cells and found to be induced by TGF-β and by epidermal growth factor (EGF), whereas EGR-α was cloned from prostate carcinoma cells and found to be induced by EGF and repressed by androgens. TIEG and EGRα have identical amino acid sequences except for 12 residues absent in the N terminus of EGRα. Thus, TIEG and EGRα appear to be encoded by the same gene. Sequence comparison between murine mGIF and these two human proteins indicates 85% amino acid identity. Comparison of their nucleotide sequences revealed that although these cDNAs are homologous within their open reading frame, more diversity exists in their 3′ untranslated regions. Both the human and murine proteins are rich in proline. mGIF has two proline-rich regions; one contains 17 prolines of 90 ...
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The following experiments were conducted to discern which domains or regions of XB130 are crucial for its Rac-dependent peripheral translocation. XB130 contains a variety of domains that in principle might contribute to its peripheral (membrane and/or lamellipodial) redistribution (Fig. 6A). Key candidate regions included the two pleckstrin homology domains, PH1 (aa 175-271) and PH2 (aa 353-446), which might be involved in the interaction between proteins and membrane phospholipids; the so called unique region (aa 491-648), which holds the lowest amino acid sequence homology to AFAP-110; the coiled-coiled motif (aa 652-750), which shows similarity to a region in AFAP-110 that harbors a leucine zipper motif for protein-protein interaction and a 17-residue stretch that is essential for F-actin binding or cross-linking; the N-terminus (aa 2-169), which contains SH3- and SH2-domain binding motifs, several tyrosine kinase target residues (e.g. Y54), as well as a putative actin-binding motif (see the ...
Structure- Type I MHC- It has a 45 KD alpha chain associated noncovalently with a 12 KD beta 2 microglobulin molecule. Alpha chain is a trans membraneglycoprotein encoded by A, B, C region in human HLA complexes and by K, D/L region in mice. Association of alpha chain and beta 2 microglobulin require for expression of class I molecule on cell membrane. Alpha chain bind to plasma membrane by its hydrophobic transmembrane segment and hydrophilic cytoplasmic tail. Alpha chain is made up of three external domain(α1,α2,α3). Each domain have 90 amino acid, a trans membrane domain have 25 hydrophobic amino acid, a short segment of hydrophilic amino acid and a cytoplasmic segment of 30 amino acid. Peptide which bind to class I MHC is made up of 8-9 amino acid ...
Whilst the fact that the single-letter codes do not all match the first letter of the amino acid that they correspond to is somewhat confusing to begin with is is worth remembering that most proteins of interest contain hundreds of amino acid residues. To illustrate how useful the amino acid codes can be lets have a look at a rather small imaginary protein with only seven residues: Alanine-Phenylalanine-Proline-Leucine-Serine-Valine-Valine-Arginine This is already irritatingly long if you have to write it out more than once. So, using the three-letter codes we have instead: ALA-PHE-PRO-LEU-SER-VAL-VAL-ARG This is already a great improvement in terms of reducing the length of the sequence that we have to write (and it remains fairly human-readable since the codes are just the first part of the amino acid names). However, if our protein had a more realistic number of residues e.g. 700 instead of 7 then this is clearly still going to be a fairly long piece of text when fully written out. Finally ...
TY - JOUR. T1 - Molecular Cloning and Primary Structure of Rat Testes Metalloendopeptidase EC 3.4.24.15. AU - Pierotti, Adrian. AU - Glucksman, Marc J.. AU - Roberts, James L.. AU - Dong, Ke Wen. AU - Pierotti, Adrian. AU - Orlowski, Marian. PY - 1990/11/1. Y1 - 1990/11/1. N2 - The complete amino acid sequence of rat testes metalloendopeptidase (EC 3.4.24.15) was deduced from the nucleotide sequence of a cDNA clone isolated by screening a rat testes library with a polyclonal antibody raised against a homogeneous preparation of the rat testes enzyme. The correctness of the sequence was verified by N-terminal amino acid sequence analysis of the isolated enzyme and by partial amino acid sequence analysis of three tryptic peptides located near the N-terminus, the middle, and C-terminus of the native protein. The enzyme is composed of 645 amino acids with a molecular weight of 72 985. This value is close to that of the purified rat testes and brain enzyme as determined by polyacrylamide gel ...
Purchase Recombinant Human NKG2-D type II integral membrane protein(KLRK1),partial (Active). It is produced in Mammalian cell. High purity. Good price.
Complete amino acid sequences were determined for thymopoietins I and II (revision), isolated from bovine thymus, and for thymopoietin III, a newly identified polypeptide isolated from bovine spleen. Thymopoietin III (TP-III) is a 49 amino acid monomeric peptide that shows minor microheterogeneity at residue 34. The three thymopoietins have largely identical sequences yet some distinct differences, suggesting very recent evolution from a common gene. The complete amino acid sequences are (Formula: see text). ...
Biology Assignment Help, Homologous proteins - amino acid sequence in fasta format, Please answer the following question on Sequence Y: Protein databases 1. What sequence from which organism is this sequence most similar to? 2. Can you find any homologues of this protein in other organisms? Can you find any clues to
Author: Geisler, N. et al.; Genre: Journal Article; Published in Print: 1983; Title: Amino acid sequence data on glial fibrillary acidic protein (GFA); implications for the subdivision of intermediate filaments into epithelial and non‐epithelial members.
9616PRTArtificial sequenceSynthetic amino acid sequence 1Leu Cys Thr Pro Ser Arg 1 5 27PRTArtificial sequenceSynthetic amino acid sequence 2Ala Ala Leu Leu Thr Gly Arg 1 5 37PRTArtificial sequenceSynthetic amino acid sequence 3Ser Gln Leu Leu Thr Gly Arg 1 5 47PRTArtificial sequenceSynthetic amino acid sequence 4Ala Ala Phe Met Thr Gly Arg 1 5 57PRTArtificial sequenceSynthetic amino acid sequence 5Ala Ala Phe Leu Thr Gly Arg 1 5 67PRTArtificial sequenceSynthetic amino acid sequence 6Ser Ala Phe Leu Thr Gly Arg 1 5 77PRTArtificial sequenceSynthetic amino acid sequence 7Ala Ser Ile Leu Thr Gly Lys 1 5 87PRTArtificial sequenceSynthetic amino acid sequence 8Val Ser Phe Leu Thr Gly Arg 1 5 97PRTArtificial sequenceSynthetic amino acid sequence 9Ala Ser Leu Leu Thr Gly Leu 1 5 107PRTArtificial sequenceSynthetic amino acid sequence 10Ala Ser Ile Leu Ile Thr Gly 1 5 117PRTArtificial sequenceSynthetic amino acid sequence 11Val Ser Phe Leu Thr Gly Arg 1 5 127PRTArtificial sequenceSynthetic amino acid ...
Autor: Peters, J. et al.; Genre: Zeitschriftenartikel; Im Druck veröffentlicht: 1987; Keywords: Amino Acid Sequence; *Bacterial Proteins/ge [Genetics]; Base Sequence; Carbohydrates/an [Analysis]; Fatty Acids/an [Analysis]; *Genes, Bacterial; *Genes, Structural; *Gram-Positive Bacteria/ge [Genetics]; Membrane Lipids/an [Analysis]; Molecular Sequence Data; Protein Processing, Post-Translational; Support, Non-U.S. Gov't; Titel: Nucleotide sequence analysis of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies
Patterns of sequence conservation between D. virilis and D. melanogaster OS-F genes suggest OBP functional domains: A comparison of OS-F protein sequences in D. melanogaster and D. virilis suggests that there are varying selective constraints across these sequences. Overall, D. melanogaster and D. virilis OS-F proteins display 76% amino acid identity. However, this identity masks a marked difference in the level of sequence conservation across the protein. The majority of nonconserved amino acids are found either at the N terminus, of which many, but not all, residues are predicted to lie within the signal sequence or in a 22-amino-acid stretch in the carboxy-terminal half of OS-F. This heterogeneous 22-aminoacid region displays only 55% amino acid identity. In contrast, the remaining portion of mature OS-F is 86% identical in these two species. Furthermore, only conservative amino acid substitutions (D-E, F-I, S-T, L-F, and I-V) are observed in OS-F residues following the first conserved ...
Amino acids refer to the molecular structure consisting of both amine and carboxyl functional groups. Referred to as alpha-amino acids in Biochemistry, typically it is defined with the formula H2NCHRCOOH where R stands for organic substitute. Amino acids can be called as the building blocks of our life.. They get combined in an unlimited number of configurations to construct all the required proteins with which our body is built. There are essentially 20 common amino acids that keep us alive, healthy and energetic. If deficiency occurs in an individual amino acid, it may create serious problem to our health system. The name of these 20 common amino acids is as follows: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalaine, proline, serine, threonine, tryptophan, tyrosine, and valine.. Alanine. It is one of the most significant among the 20 common amino acids. It offers energy to your system. It ...
The main transporting protein for vitamin A in rabbit serum, the retinol-binding protein (RBP), was isolated and its amino acid sequence determined. Rabbit RBP was found to be highly homologous to human RBP, whose amino acid sequence was elucidated earlier, and to rat RBP. The rat RBP sequence was obtained by combining information deduced from the nucleotide sequences of two overlapping cDNA clones with the NH2-terminal sequence of the isolated protein determined by automated Edman degradation. The identity between the three proteins is approximately 90%. The high degree of homology between RBP molecules from different species is probably explained by the fact that RBP participates in at least three types of molecular interactions: in the binding of prealbumin, in the interaction with retinol, and in the recognition of a specific cell surface receptor. All these interactions should lead to a conservation of RBP structure. The amino acid differences between rabbit, rat, and human RBP are discussed in
A short sequence of predominantly basic amino acids Pro-Pro-Lys-Lys-Lys-Arg-Lys-Val from SV40 Large T is responsible for the normal nuclear location of the protein. Alteration of Lys-128 to each of six different residues other than Arg renders Large T cytoplasmic, whereas single amino acid changes in the surrounding region impair but do not prevent nuclear accumulation. When transposed to the amino terminus of cytoplasmic Large T species, or Escherichia coli β-galactosidase or of chicken muscle pyruvate kinase, the sequence around Lys-128 of Large T is able to direct the recipient protein to the nucleus. This demonstrates that these amino acids can be sufficient for nuclear location and can act as a nuclear location signal. A computer search of over 2500 proteins reveals that some other nuclear proteins (for example, BK virus Large T, SV40 VP2 and adenovirus 72kDa DNA binding protein) contain very similar basic tracts, but so too do some presumed non-nuclear proteins (for example, poliovirus ...
Mc kean, D J.; Potter, M; and Hood, L, Amino acid sequence comparison of three new balb/c mouse kappa chains. Abstr. (1972). Subject Strain Bibliography 1972. 679 ...
We report the sequence of a 4.5-kb cDNA clone isolated from a human melanoma library which bears high amino acid sequence identity to the yeast mitochondrial (mt) DNA polymerase (Mip1p). This cDNA contains a 3720-bp open reading frame encoding a predicted 140-kDa polypeptide that is 43% identical to Mip1p. The N-terminal part of the sequence contains a 13 glutamine stretch encoded by a CAG trinucleotide repeat which is not found in the other DNA polymerases gamma (Pol gamma). Multiple amino acid sequence alignments with Pol gamma from Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris, Drosophila melanogaster, Xenopus laevis and Mus musculus show that these DNA polymerases form a family strongly conserved from yeast to man and are only loosely related to the Family A DNA polymerases. ...
Abstract: Recognition of the phosphorylation sites in proteins is required for reconstruction of regulatory processes in living systems. This task is complicated because the phosphorylation motifs in amino acid sequences are considerably degenerated. To improve the prediction efficacy researchers often use additional descriptors, which should reflect physicochemical features of site-surrounding regions. We have evaluated the reasonability of this approach by applying molecular descriptors (MNA) for structural presentation of the peptide segments. Comparative testing was performed using the prognostic method PASS and two input data types: sets of the MNA descriptors represented peptides as chemical structures and amino acid sequences written using a one-letter code. Training sets were classified in accordance with the established types of the enzymes (protein kinases), modifying corresponding phosphorylation sites. The accuracy estimates obtained by prognosis validation for various classes of ...
We have studied two related proteins that contain a repeated amino acid motif homologous to the anti-angiogenic type 1 repeats of thrombospondin-1 (TSP1). Complete sequence analysis revealed no other similarities with TSP1, but identified unique signal sequences, as well as metalloprotease and disintegrin-like domains in the NH(2) termini. We named these proteins METH-1 and METH-2 due to the novel combination of metalloprotease and thrombospondin domains. Overall amino acid sequence identity between METH-1 and METH-2 is 51. 7%, yet transcript distribution revealed non-overlapping patterns of expression in tissues and cultured cell lines. To characterize these proteins functionally, we isolated full-length cDNAs, produced recombinant protein, and generated antisera to the recombinant proteins. Both METH-1 and METH-2 represent single copy genes, which encode secreted and proteolytically processed proteins. METH proteins suppressed fibroblast growth factor-2-induced vascularization in the cornea pocket
The carboxyl-terminal sequences of the two polypeptide chains of the Saccharomyces cerevisiae K1 killer toxin were determined by protein sequencing and amino acid analysis of peptide fragments generated from the mature, secreted toxin. The COOH-terminal amino acid of the beta chain is histidine 316, the final residue encoded by the precursor gene. The COOH terminus of the alpha chain is at alanine 147 of the preprotoxin. Amino acid composition data for the purified toxin are consistent with that predicted from the gene sequence of the preprotoxin where the alpha and beta subunits consist of amino acid residues 45-147 and 234-316, respectively. The molecular weight of the mature alpha beta dimer is about 20,658. The COOH-terminal sequence determination completes the location of the toxin subunits in the precursor, and its configuration may be represented as prepropeptide-Pro-Arg-alpha-Arg-Arg-gamma-Lys-Arg-beta, where gamma represents the interstitial glycosylated peptide. The COOH terminal side of the
Chemical modification using thiol-directed agents and site-directed mutagenesis have been used to investigate the crucial role of an active site cysteine residue within the substrate-binding domain of human type I Ins(1,4,5)P3 5-phosphatase. Irreversible inhibition of enzymic activity is provoked by chemical modification of the enzyme by N-ethylmaleimide (NEM), 5,5´-dithio-2-nitrobenzoic acid, iodoacetate and to a much smaller extent by iodoacetamide. The alkylation reaction by NEM is prevented in the presence of Ins(1,4,5)P3. The results indicate that NEM binds at the active site of the enzyme with a stoichiometry of 0.9 mol of NEM per mol of enzyme. A single [14C]NEM-modified peptide was isolated after α-chymotrypsin proteolysis of the radiolabelled enzyme and reverse-phase HPLC. Sequence analysis of the active site-labelled peptide (i.e. MNTRCPAWCD) demonstrated that Cys348 contained the radiolabel. Furthermore two mutant enzymes were obtained by site-directed mutagenesis of the cysteine ...
Roswit W.T., McCourt D.W., Partridge N.C., Jeffrey J.J.. Two protein inhibitors of metalloproteinases (TIMP) were isolated from medium conditioned by the clonal rat osteosarcoma line UMR 106-01. Initial purification of both a 30-kDa inhibitor and a 20-kDa inhibitor was accomplished using heparin-Sepharose chromatography with dextran sulfate elution followed by DEAE-Sepharose and CM-Sepharose chromatography. Purification of the 20-kDa inhibitor to homogeneity was completed with reverse-phase high-performance liquid chromatography. The 20-kDa inhibitor was identified as rat TIMP-2. The 30-kDa inhibitor, although not purified to homogeneity, was identified as rat TIMP-1. Amino terminal amino acid sequence analysis of the 30-kDa inhibitor demonstrated 86% identity to human TIMP-1 for the first 22 amino acids while the sequence of the 20-kDa inhibitor was identical to that of human TIMP-2 for the first 22 residues. Treatment with peptide:N-glycosidase F indicated that the 30-kDa rat inhibitor is ...
Author: Schödel, Florian et al.; Genre: Journal Article; Published in Print: 1988; Title: Letter to the Editor : Amino Acid Sequence Similarity Between Retroviral and E. coli RNase H and Hepadnaviral Gene Products
Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.. cDNA clones of two novel Ras-related GTP-binding proteins (RagA and RagB) were isolated from rat and human cDNA libraries. Their deduced amino acid sequences comprise four of the six known conserved GTP-binding motifs (PM1, -2, -3, G1), the remaining two (G2, G3) being strikingly different from those of the Ras family, and an unusually large C-terminal domain (100 amino acids) presumably unrelated to GTP binding. RagA and RagB differ by seven conservative amino acid substitutions (98% identity), and by 33 additional residues at the N terminus of RagB. In addition, two isoforms of RagB (RagBs and RagB1) were found that differed only by an insertion of 28 codons between the GTP-binding motifs PM2 and PM3, apparently generated by alternative mRNA splicing. Polymerase chain reaction amplification with specific primers indicated that both long and short form of RagB transcripts were present in adrenal gland, thymus, spleen, and kidney, ...
Start Over You searched for: Formats Text ✖Remove constraint Formats: Text Subjects Amino Acid Sequence ✖Remove constraint Subjects: Amino Acid Sequence Subjects Molecular Sequence Data ✖Remove constraint Subjects: Molecular Sequence Data Titles Hox-1.11 and Hox-4.9 Homeobox Genes ✖Remove constraint Titles: Hox-1.11 and Hox-4.9 Homeobox Genes Publication Year 1992 ✖Remove constraint Publication Year: 1992 ...
The two cotranslational processes, cleavage of N‐terminal methionine residues and N‐terminal acetylation, are by far the most common modifications, occurring on the vast majority of proteins. Proteins from prokaryotes, mitochondria and chloroplasts initiate with formylmethionine, whereas proteins from the cytosol of eukaryotes initiate with methionine. The formyl group is removed from prokaryotic proteins by a deformylase, resulting in methionine at the N‐termini. The methionine at the N‐termini is cleaved from nascent chains of most prokaryotic and eukaryotic proteins. N‐terminal acetylation occurs subsequently on certain of the proteins, either containing or lacking the methionine residue. This N‐terminal acetylation occurs on more than one‐half of eukaryotic proteins, but seldom on prokaryotic proteins (Driessen et al., 1985; Kendall et al., 1990).. Because the N‐terminal region of yeast iso‐1‐cytochrome c (iso‐1) is dispensable for biosynthesis, function and ...
Alazawi W, Heath H, et al. Stat2 loss leads to cytokine-independent, cell-mediated lethality in LPS-induced sepsis. Proc Natl Acad Sci U S A 110(21):8656-8661, 2013 [95].. Arnold, ES, SC Ling, et al. ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP- 43. Proc Natl Acad Sci U S A 110(8):E736- E745, 2013 [96].. Burdick RC, Hu WS, Pathak VK. Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes. Proc Natl Acad Sci U S A 110(49):E4780-E4789, 2013 [97].. Chen J, Feigenbaum L, et al. Insulin-dependent diabetes induced by pancreatic beta cell expression of IL-15 and IL-15R alpha. Proc Natl Acad Sci U S A 110(33):13534- 13539, 2013 [98].. Feng MQ, Gao W, et al. Therapeutically targeting glypican-3 via a conformation-specific single-domain antibody in hepatocellular carcinoma. Proc Natl Acad Sci U S A 110(12):E1083-E1091, 2013 [99].. Kim TS, Park JE, Shukla A, Choi S, Murugan RN, Lee JH, Ahn M, Rhee K, ...
The omc gene, encoding the outer membrane protein-macromolecular complex (OMP-MC), was cloned in two pieces from Neisseria gonorrhoeae 2686. The 5 fragment of the omc gene included a promoter sequence, as indicated by its unregulated expression in Escherichia coli. Attempts to reconstruct an intact omc gene were unsuccessful, suggesting that expression of the complete OMP-MC protein was toxic to E. coli. Complete sequence determination revealed a coding sequence of 2,133 nucleotides; the deduced amino acid sequence indicated a mature protein of 687 amino acids with an NH2-terminal signal peptide of 24 amino acids. Analysis of the deduced amino acid sequence revealed that the NH2-terminal half of OMP-MC is generally hydrophilic, while the COOH-terminal portion contains alternating hydrophobic and hydrophilic regions. Serological analyses demonstrated that the NH2-terminal portion of OMP-MC is exposed on the gonococcal surface and the COOH-terminal portion is membrane associated. ...
TY - JOUR. T1 - RevTrans: multiple alignment of coding DNA from aligned amino acid sequences. AU - Wernersson, Rasmus. AU - Pedersen, Anders Gorm. PY - 2003. Y1 - 2003. N2 - The simple fact that proteins are built from 20 amino acids while DNA only contains four different bases, means that the signal-to-noise ratio in protein sequence alignments is much better than in alignments of DNA. Besides this information-theoretical advantage, protein alignments also benefit from the information that is implicit in empirical substitution matrices such as BLOSUM-62. Taken together with the generally higher rate of synonymous mutations over non-synonymous ones, this means that the phylogenetic signal disappears much more rapidly from DNA sequences than from the encoded proteins. It is therefore preferable to align coding DNA at the amino acid level and it is for this purpose we have constructed the program RevTrans. RevTrans constructs a multiple DNA alignment by: (i) translating the DNA; (ii) aligning ...
Exported prokaryotic proteins typically contain an amino-terminal extension called the signal peptide. Although signal sequences display little primary sequence homology, they share features which promote secretion through the same pathway. These characteristics include a net positive charge in the amino-teminus, a hydrophobic core with $\alpha$-helical propensity, and a cleavage region which contains small side chain residues in the $-$1 and $-$3 positions. The goals of this research are to further analyze the requirement for each property, to determine whether the different features operate at concurrent steps and, ultimately, to correlate the physical features with their functional role(s).^ The alkaline phosphatase signal sequence represents a typical signal peptide and serves as a prototype for designing mutants with simplified sequences that facilitate the delineation of the required physical features. A series of signal sequences varying in amino terminal charge and core region hydrophobicity
A human tumor necrosis factor (TNF) binding protein from serum of cancer patients was purified to homogeneity and partially sequenced. Synthetic DNA probes based on amino acid sequence information were used to isolate cDNA clones encoding a receptor for TNF. The TNF receptor (TNF-R) is a 415 amino acid polypeptide with a single membrane-spanning region. The extracellular cysteine-rich domain of the TNF-R is homologous to the nerve growth factor receptor and the B cell activation protein Bp50. Human embryonic kidney cells transfected with a TNF-R expression vector specifically bind both 125I-labeled and biotinylated TNF-alpha. Unlabeled TNF-alpha and TNF-beta were equally effective at displacing the binding of labeled TNF-alpha to TNF-R expressing cells. Northern analysis indicates a single species of mRNA for the TNF-R in a variety of cell types. Therefore, the soluble TNF binding protein found in human serum is probably proteolytically derived from the TNF-R. ...
Examples of such classifications, generico do remedio evista some of which overlap include, nonpolar (ie, hydrophobic) amino acid residues can include alanine (Ala or A), leucine (Leu or L), isoleucine (Ile or I), valine (Val or V), proline (Pro or P), phenylalanine (Phe or F), tryptophan (Trp or W) and methionine (Met or M); polar neutral amino acid residues can include glycine (Gly or G), serine (Ser or S), threonine (Thr or T), cysteine (Cys or C), tyrosine (Tyr or Y), asparagine (Asn or N) and glutamine (Gln or Q); small amino acids include glycine (Gly or G), and alanine (Ala or A); hydrophobic amino acid residues can include valine (Val or V), leucine (Leu or L), isoleucine (Ile or I), methionine (Met or M), and proline (Pro or P); nucleophilic amino acids can include serine (Ser or S), threonine (Thr or T), and cysteine (Cys or C); aromatic amino acids can include phenylalanine (Phe or F), tyrosine (Tyr or Y), and tryptophan (Trp or W); amide amino acids can include asparagine (Asn or N), ...
New YorkCrossRefGoogle ScholarDayhoff MO, download Teaching Harry Potter: The science, Park CM( 1972) A player of technological club in causes. so: Dayhoff MO( research) performance of theory pp. and education, archaeological edn. National Biomedical Research Foundation, Washington, DCGoogle Scholarde AlencarFigueiredo LF, Sine B, Chantereau J et al( 2010) material of implementation god in conspiracy: method with Money in Sh2, Bt2, SssI, Ae1, Wx and O2. 1185CrossRefGoogle ScholarEyras E, Reymond A, Castelo R, Bye JM, Camara F, Flicek information, Huckle EJ, Parra G, Shteynberg DD, Wyss C, Rogers J, Antonarakis SE, Birney E, Guigo R, Brent MR( 2005) Gene project in the prediction minister. BMC Bioinforma 6(1):131CrossRefGoogle ScholarGill BS, Appels R, Botha-Oberholster AM et al( 2004) A read representation on rationale policy Breaking: challenging performance age on basis journal. 1096CrossRefPubMedCentralPubMedGoogle ScholarGnerrea S, MacCallum I, Przybyiski D et al( 2011) sentence device ...
Human cellular nucleic acid binding protein (CNBP) is a zinc finger DNA binding protein of unknown function. The human CNBP cDNA was used as a probe to isolate four structurally distinct but highly homologous mouse liver cDNA clones. Each of the mouse clones exhibited extraordinary sequence conservation with human CNBP cDNA, and the predicted mouse amino acid sequence identities with human CNBP protein ranged from 99 to 100%. Genetic mapping of CNBP genes in interspecific and intersubspecific mouse backcrosses revealed two loci that hybridize to CNBP cDNA at high stringency, located on chromosomes 5 and 6. The subcellular distribution of the CNBP protein was characterized with a specific polyclonal antibody generated against a synthetic peptide from the carboxyl terminus. CNBP was found in the cytosol and the endoplasmic reticulum in subcellular fractions from mouse liver, but was undetectable in nuclear fractions. These data suggest that CNBP is a member of a highly conserved family of
Short-chain dehydrogenases/reductases form a large, evolutionarily old family of NAD(P)(H)-dependent enzymes with over 60 genes found in the human genome. Despite low levels of sequence identity (often 10-30%), the three-dimensional structures display a highly similar alpha/beta folding pattern. We have analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3beta/17beta-hydroxysteroid dehydrogenase and selected mutants. Structure determination of the wild-type enzyme at 1.2-A resolution by x-ray crystallography and docking analysis was used to interpret the biochemical data. Enzyme kinetic data from mutagenetic replacements emphasize the critical role of residues Thr-12, Asp-60, Asn-86, Asn-87, and Ala-88 in coenzyme binding and catalysis. The data also demonstrate essential interactions of Asn-111 with active site residues. A general role of its side chain interactions for maintenance of the active site configuration to
MGI protein superfamily detail pages represent the protein classification set for a homeomorphic superfamily from the Protein Information Resource SuperFamily (PIRSF) site.. Mouse superfamily members are shown with links to their corresponding HomoloGene Classes. Note that pseudogenes are included in PIRSF families but not in orthology sets used here. You can select a given mouse superfamily member and download (or forward to NCBI BLAST) FASTA formatted protein sequences of that mouse gene and its mouse, human and rat homologs, as defined in the corresponding HomoloGene Class. The numbers of mouse, human and rat genes in the HomoloGene Class are shown. You can also Select all mouse superfamily members to obtain their protein sequences and the protein sequences for all mouse, human and rat homologs of the mouse superfamily members.. The number of protein sequences returned does not always match the numbers of homologs shown, because the same protein sequence can be associated with multiple ...
1. Monoclonal antibody binding to human CD40, comprising (i) two heavy chains, each of which contains a constant region derived from human IgG4, with the substitution of serine with Proline at position 228 and the substitution of LEU is in glutamic acid at position 235, and the variable region of the heavy chain of the monoclonal antibody produced by hybridoma 4D11 (no access FERM BP-7758), and (ii) two light chains, each of which contains the variable region of the light chain of the monoclonal antibodies produced by hybridoma 4D11 (no access FERM BP-7758).. 2. Monoclonal antibody binding to human CD40, comprising (i) two heavy chains, each of which contains a constant region derived from human IgG4, with the substitution of serine with Proline at position 228 and the substitution of leucine glutamic acid at position 235, and variable region represented by amino acid sequence in the range from Q at position 27 to S at position 147 in SEQ ID NO:46, and (ii) two light chains, each of which ...
Аннотация доклада: A new algorithm Zebra and a corresponding web-server have been developed to systematically study diverse protein superfamilies and identify the subfamily-specific positions (SSPs) - conserved only within functional subfamilies but different between them - that seem to be responsible for different substrate specificity, catalytic activity, stability, etc. [1]. It is known from experimental enzymology that mutations in the active site can change enantioselectivity, substrate specificity and catalytic promiscuity more effectively than distant ones. However, both close and distant mutations can be important for activity and stability thus highlighting complexity of evolutionary adaptation. Therefore, to identify functionally important SSPs a novel scoring function is suggested that incorporates structural information as well as physicochemical and residue conservation in protein subfamilies. The algorithm does not require pre-defined subfamilies and can propose ...
We propose hierarchical motif vectors to represent local amino acid sequence configurations for predicting the functional attributes of amino acid sites on a global scale in a quasi-supervised learning framework. The motif vectors are constructed via wavelet decomposition on the variations of physico-chemical amino acid properties along the sequences. We then formulate a prediction scheme for the functional attributes of amino acid sites in terms of the respective motif vectors using the quasi-supervised learning algorithm that carries out predictions for all sites in consideration using only the experimentally verified sites. We have carried out comparative performance evaluation of the proposed method on the prediction of N-glycosylation of 55,184 sites possessing the consensus N-glycosylation sequon identified over 15,104 human proteins, out of which only 1,939 were experimentally verified N-glycosylation sites. In the experiments, the proposed method achieved better predictive performance ...
Stanniocalcins (STCs) represent small glycoprotein hormones, found in all vertebrates, which have been functionally implicated in Calcium homeostasis. However, recent data from mammalian systems indicated that they may be also involved in embryogenesis, tumorigenesis and in the context of the latter especially in angiogenesis. Human STC1 is a 247 amino acids protein with a predicted molecular mass of 27 kDa, but preliminary data suggested its di- or multimerization. The latter in conjunction with alternative splicing and/or post-translational modification gives rise to forms described as STC50 and big STC, which molecular weights range from 56 to 135 kDa. In this study we performed a biochemical and structural analysis of STC1 with the aim of obtaining low resolution structural information about the human STC1, since structural information in this protein family is scarce. We expressed STC1 in both E. coli and insect cells using the baculo virus system with a C-terminal 6 × His fusion tag. From the
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The IC 50 (concentration of drug causing 50% growth inhibition) was then calculated! Examples of such classifications, protonix where to buy some of which overlap include, nonpolar (ie, hydrophobic) amino acid residues can include alanine (Ala or A), leucine (Leu or L), isoleucine (Ile or I), valine (Val or V), proline (Pro or P), phenylalanine (Phe or F), tryptophan (Trp or W) and methionine (Met or M); polar neutral amino acid residues can include glycine (Gly or G), serine (Ser or S), threonine (Thr or T), cysteine (Cys or C), tyrosine (Tyr or Y), asparagine (Asn or N) and glutamine (Gln or Q); small amino acids include glycine (Gly or G), and alanine (Ala or A); hydrophobic amino acid residues can include valine (Val or V), leucine (Leu or L), isoleucine (Ile or I), methionine (Met or M), and proline (Pro or P); nucleophilic amino acids can include serine (Ser or S), threonine (Thr or T), and cysteine (Cys or C); aromatic amino acids can include phenylalanine (Phe or F), tyrosine (Tyr or Y), ...
A tonoplast protein of 31 kDa apparent molecular mass (TpP 31) was isolated from two-dimensional gels. Amino acid sequences were determined from LysC endoproteinase-peptide fragments. Using degenerate oligonucleotides, a corresponding cDNA clone of 1034 bp was isolated from a barley leaf cDNA library. It encodes for subunit E of the vacuolar H+-ATPase, the first one identi fled in plants so far. The open reading frame extends over 681 bp, encoding a gene product of 227 amino acids and a calculated molecular weight of 26 228 g mol(-1). Northern and Western blot analysis indicates constitutive expression of subunit E in all plant organs with only small effects of salt stress. Localization of TpP 31 at the tonoplast was confirmed in fractions of purified vacuolar membrane obtained by free-flow electrophoresis. Immunoprecipitation of newly synthesized S-35-labelled membrane proteins with anti-TpP 31 gave two additional bands with apparent molecular masses of about 53 and 62 kDa. Gel filtration after ...
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Cytochrome P-450 catalyzed reactions are extremely important in the metabolic pathways of both pro- and eucaryotes. Detailed mechanistic understanding of this superfamily, however, has been hampered by the availability of only one well characterized procaryotic system. Preliminary characterization of cytochrome P-450lin (P-450lin), the enzyme responsible for the 8-methyl hydroxylation of linalool as the first committed step of Pseudomonas incognitas utilization of that substrate as its sole carbon source, indicates its importance in expanding the foundation of the P-450 superfamily. Paramount to detailed mechanistic dissection, however, is the availability of a genetic handle, reagent quantities of pure enzyme and a reliable tertiary structure. Herein, we describe the realization of the first two goals which should aid in the completion of the third. Utilizing a Polymerase Chain Reaction-based cloning strategy based on the P-450lin NH$\sb2$-terminal and tryptic-fragment amino acid sequence, the ...
The DNA sequence of the whole of the short unique region (U S ) and that of part of the short terminal repeat (TR S ) of herpesvirus of turkeys (HVT) were determined. HVT U S is 8·6 kbp long and contains eight potential open reading frames (ORFs). Seven of these have counterparts in the U S of herpes simplex virus type 1 (HSV-1). The homologous proteins include US1, US2, US10, protein kinase (US3) and the glycoproteins gD, gI and gE. In addition, HVT contains one ORF which has a counterpart in the U S of Marek's disease virus (MDV) but is not homologous to any other known herpesvirus gene. Although HVT and MDV proteins encoded by U S genes have evident similarities with proteins encoded by alphaherpesviruses, multiple alignment analysis of predicted amino acid sequences show that HVT proteins are more closely related to MDV proteins than to homologous proteins of mammalian alphaherpesviruses. The percentage amino acid identity between HVT and MDV U S -encoded proteins ranges from 35 to 65, the
A novel gene, Xin, from chick (cXin) and mouse (mXin) embryonic hearts, may be required for cardiac morphogenesis and looping. Both cloned cDNAs have a single open reading frame, encoding proteins with 2,562 and 1,677 amino acids for cXin and mXin, respectively. The derived amino acid sequences share 46% similarity. The overall domain structures of the predicted cXin and mXin proteins, including proline-rich regions, 16 amino acid repeats, DNA-binding domains, SH3-binding motifs and nuclear localization signals, are highly conserved. Northern blot analyses detect a single message of 8.9 and 5.8 kilo base (kb) from both cardiac and skeletal muscle of chick and mouse, respectively. In situ hybridization reveals that the cXin gene is specifically expressed in cardiac progenitor cells of chick embryos as early as stage 8, prior to heart tube formation. cXin continues to be expressed in the myocardium of developing hearts. By stage 15, cXin expression is also detected in the myotomes of developing ...
Proteins are lairge biological molecules, or macromolecules, consistin o ane or mair chains o amino acid residues. Proteins perform a vast array o functions athin organisms, includin catalysin metabolic reactions, DNA replication, respondin tae stimuli, an transportin molecules frae ane location tae anither. Proteins differ frae ane anither primarily in thair sequence o amino acids, that is dictatit bi the nucleotide sequence o thair genes, an that uisually results in protein foldin intae a speceefic three-dimensional structur that determines its acteevity. A linear cheen o amino acid residues is cried a polypeptide. A protein conteens at least ane lang polypeptide. Short polypeptides, conteenin less nor 20-30 residues, are rarely conseedert tae be proteins an are commonly cried peptides, or whiles oligopeptides. The individual amino acid residues are bondit thegither bi peptide bonds an adjacent amino acid residues. The sequence o amino acid residues in a protein is defined bi the sequence o a ...
TY - JOUR. T1 - Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial. AU - Caplan, Michael. AU - Schwartzfarb, Elissa M.. AU - Zhang, Shuguang. AU - Kamm, Roger D.. AU - Lauffenburger, Douglas A.. PY - 2002. Y1 - 2002. N2 - In order to elucidate design principles for biocompatible materials that can be created by in situ transformation from self-assembling oligopeptides, we investigate a class of oligopeptides that can self-assemble in salt solutions to form three-dimensional matrices. This class of peptides possesses a repeated sequence of amino acid residues with the type: hydrophobic/negatively-charged/hydrophobic/positively-charged. We systematically vary three chief aspects of this sequence type: (1) the hydrophobic side chains; (2) the charged side chains; and (3) the number of repeats. Each of these has been previously shown to influence the self-assembly properties of these materials. Employing a rheometric ...
Predicting the function of newly discovered proteins by simply inspecting their amino acid sequence is one of the major challenges of post-genomic computational biology, especially when done without recourse to experimentation or homology information. Machine learning classifiers are able to discriminate between proteins belonging to different functional classes. Until now, however, it has been unclear if this ability would be transferable to proteins of unknown function, which may show distinct biases compared to experimentally more tractable proteins. Here we show that proteins with known and unknown function do indeed differ significantly. We then show that proteins from different bacterial species also differ to an even larger and very surprising extent, but that functional classifiers nonetheless generalize successfully across species boundaries. We also show that in the case of highly specialized proteomes classifiers from a different, but more conventional, species may in fact outperform the
TOC: Baldwin boosters, Baldwin skeptics , Baldwin and his many effects / David J. Depew , Baldwin effects and the expansion of the explanatory repertoire in evolutionary biology / Stephen M. Downes , Between Baldwin skepticism and Baldwin boosterism / Peter Godfrey-Smith , The Baldwin effect: a crane, not a skyhook / Daniel Dennett , Multilevel selection in a complex adaptive system: the problem of language origins / Terrence W. Deacon , Postscript on the Baldwin effect and niche construction / Peter Godfrey-Smith, Daniel Dennett, and Terrence W. Deacon , Evolution, development, and the individual acquisition of traits: what weve learned since Baldwin / Celia L. Moore , Baldwin and beyond: organic selection and genetic assimilation / Brian K. Hall , On having a hammer / Susan Oyama , Beyond the Baldwin effect: James Mark Baldwins Social Heredity, epigenetic inheritance, and niche construction / Paul E. Griffiths , The Baldwin effect in the age of computation / Ruben R. Puentedura , Role of ...
Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells, and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of ...