• Cysteine residues at position 128 and 208 form a disulfide bond. (wikipedia.org)
  • The cysteine residues form a disulfide bond. (orangepeptide.com)
  • Paired cysteine substitutions were made at amino acids predicted to form inter-monomer disulfide cross-links, and these substitutions were capable of forming flagella when transfected into a flagellin-negative strain of Salmonella enterica subspecies Typhimurium. (biomedcentral.com)
  • We identified amino acid pairs, with cysteine substitutions, were able to form intermolecular disulfide bonds that stabilized the resulting flagellar filaments in detergent, hydrochloric acid, and high temperatures while retaining its immunostimulatory function. (biomedcentral.com)
  • Amino acid differences compared with the consensus were visualized with Highlighter software ( https://www.hiv.lanl.gov/content/sequence/HIGHLIGHT/highlighter_top.html ). (cdc.gov)
  • The third difference is the very high proportion of proline residues in the sequence accounting for about one-third of the sequence. (springer.com)
  • Together, these results indicate that the structure of the rhodopsin N terminus must be maintained by an appropriate amino acid sequence surrounding N2 and may require a carbohydrate moiety at N15. (jneurosci.org)
  • 1115 The position of the amino-acid change on the UniProtKB canonical protein sequence. (expasy.org)
  • IDSQVLCGAVKWLILEKQKP D GVFQEDAPVIHQEMIGGLRN The residue change on the sequence. (expasy.org)
  • Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown. (expasy.org)
  • The nucleotide sequence analysis of nonstructural protein 2 gene of EDRD1 and comparison with Vietnamese HP-PRRSV showed that the 39 amino acid deletion sites of EDRD1 was nearly in the same region as the 29 amino acid deletion sites of HP-PRRSV. (biomedcentral.com)
  • The inferred amino acid sequence predicts a 125,513 dalton protein that contains 17 potential N-linked glycosylation sites and is unusually rich in tyrosine and asparagine residues. (silverchair.com)
  • A 1% sequence variability among different isolates of the pathogenic strain HM1:IMSS and a 12-13% variability between pathogenic and nonpathogenic strains are revealed by comparison to published partial amino acid sequences (Tannich, E., R.D. Horstmann, J. Knobloch, and H.H. Arnold. (silverchair.com)
  • The currently available implementation for this method initially defines interfacial residues using atomic details, and then uses positions of the Cα atoms for structural alignment and scoring, and includes a sequence-order dependent version [ 10 ] and a sequence-order independent version [ 11 ]. (biomedcentral.com)
  • In N-linked glycosylation, oligosaccharides are attached to the amide nitrogen of an asparagine (Asn) residue in a consensus sequence Asn-X-Ser/Thr where X is any amino acid except proline. (themedicinemaker.com)
  • For sequences with a typical fraction of hydrophobic residues, we impact on how permissive with respect to sequence specificity find that the nonrandomness can be interpreted as anticorrela- the protein folding process is-- only sequences with nonran- tions. (lu.se)
  • Almost all the amino acids undergo the process of PTMs, except leucine (L), isoleucine (I), valine (V), alanine (A) and phenylalanine (F) [2]. (deepdyve.com)
  • Site-directed mutagenesis of the γ-aminobutyric acid type A (GABA A ) receptor β 2 subunit has demonstrated that conversion of a conserved glycine residue located at the entrance to the first transmembrane domain into the homologous ρ 1 residue phenylalanine alters the modulating effects of four different i.v. anesthetics: pentobarbital, alphaxalone, etomidate, and propofol. (aspetjournals.org)
  • The AmTrac sensors differ only by two residues at the N-terminus of the cpEGFP, also referred to as left linker, the right linker being composed of phenylalanine (F) and asparagine (N) in all sensors. (elifesciences.org)
  • The locations of proteins and variant amino acid residues are shown at top. (cdc.gov)
  • posttranslational modifications, amino acid variations, computational mutation analysis, protein PTM predictor, network biology Introduction Protein PTMs are biochemical alterations of amino acids that change the physicochemical properties of target proteins, leading to structural changes and therefore regulating protein-protein interactions and cellular signal transduction in developmental and cancer pathways [1]. (deepdyve.com)
  • 7] analyzed amino acid variations of 15 different PTMs and indicated that about 4.5% of amino acid variations may affect protein function through disruption of PTMs, and the mutation of 238 PTMs sites in human proteins was causative of disease. (deepdyve.com)
  • However, it often requires extensive laboratory work and considerable expense to make thousands of variant proteins and select amino acid variations that influence PTM sites. (deepdyve.com)
  • Furthermore, the ferredoxin used and the identity of the variable motif residue in these proteins affects the functionality of the monooxygenase system and has a significant influence on the redox properties of the ferredoxins. (rsc.org)
  • These differences in the amino acids' properties are likely to change the proteins' structure as this residue is located in a helix and therefore this mutation is very likely to affect the protein's function. (tu-muenchen.de)
  • Our analysis has been the amino acid sequences in proteins differ from what is carried out using two different methods, which differ substantially expected from random sequences in a statistically significant from what is used in ref. 3, although the starting point is similar. (lu.se)
  • PROT data base (6) of functional proteins, this method yields model containing only two amino acid types, hydrophobic and clear evidence for nonrandomness. (lu.se)
  • To under- denoted the AB model, consists of chains of two kinds of stand the statistical distribution of hydrophobicity along proteins ``amino acids'' interacting with Lennard-Jones potentials. (lu.se)
  • These results suggest that the first transmembrane glycine residue on the β 2 subunit may be important for conformational or allosteric interactions of channel gating by both GABA and anesthetics. (aspetjournals.org)
  • indicates a variable amino acid residue. (rsc.org)
  • The location of this amino acid at the extracellular end of the second transmembrane segment, its influence in both homomeric and heteromeric receptor function, and its dominant behavior suggest that this residue of the beta subunit is involved in an allosteric modulation of the receptor. (nih.gov)
  • Our laboratory has shown that up to 40 carboxy terminal residues of each subunit contribute to the stabilization of tetramers (R.M. Blong, E. Bedows, O. Lockridge, The tetramerization domain of butyrylcholinesterase is at the carboxy-terminus, Biochem. (inrae.fr)
  • Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. (lbl.gov)
  • Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. (lbl.gov)
  • In addition, these amino acid mutations altered the VRC01 susceptibility of many AE-Env clones. (biomedcentral.com)
  • To better define the residues which participate in tetramer stabilization, the in vivo interaction of the BChE C-terminus 46 residue peptide was quantitated for wild type and mutant BChE using the yeast two-hybrid system. (inrae.fr)
  • However, only 11.7% of the interaction seen with the wild type peptide was observed with the mutant in which seven conserved aromatic residues (Trp 543, Phe 547, Trp 550, Tyr 553, Trp 557, Phe 561, and Tyr 564) had been altered to alanines (aromatics off mutant). (inrae.fr)
  • Oxytocin is a peptide of nine amino acids (a nonapeptide). (orangepeptide.com)
  • Glycosylation is an enzymatic process involving the addition of oligosaccharide structures to specific amino acid sites of polypeptides to form glycoproteins. (themedicinemaker.com)
  • PNGase F cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid and complex oligosaccharides from N -linked glycoproteins (5), as shown in Figure 2. (neb.com)
  • The glycan core structure (see Figure 1) presented by antibodies contains N-acetylglucosamine (GlcNAc) and mannose upon which other sugar residues, such as galactose, sialic acid and fucose, are added. (themedicinemaker.com)
  • Other commonly used endoglycosidases such as Endoglycosidase H ( NEB #P0702 ) are not suitable for general deglycosylation of N -linked sugars, because it only deglycosylates glycoproteins containing primarily high mannose N -linked structures, as well as leaving one N -acetylglucosamine residue attached to the asparagine. (neb.com)
  • The major role of the NA is to release new progeny virions from an infected cell by enzymatically cleaving sialic acid receptors, which aids virus spread to uninfected cells within an infected host. (cdc.gov)
  • These observations suggest that the stabilization of BChE tetramers is mediated through the interaction of the seven conserved aromatic residues, Trp 543, Phe 547, Trp 550, Tyr 553, Trp 557, Phe 561, and Tyr 564, and that the poly-L-proline induced increase in tetrameric BChE is mediated through these seven aromatic residues. (inrae.fr)
  • For structural analysis of asparagine-linked carbohydrates, sugars are released from the protein backbone by enzymes such as PNGase F ( NEB #P0704 ). (neb.com)
  • Murine gamma-aminobutyric acid (GABA) type A homomeric receptors made of beta1 subunits are profoundly different, when expressed in Xenopus oocytes, from beta3 homomeric receptors. (nih.gov)
  • Through construction of chimeric beta1/beta3 receptors, we identified a single amino acid that determines the pharmacological difference between the two beta subunits. (nih.gov)
  • In alpha1betax or alpha1betaxgamma2 heteromeric receptors, the same residue manifests as a partial determinant of the degree of potentiation of the GABA-induced current by some general anesthetics. (nih.gov)
  • Analysis of this HA gene shows that it is closely related to avian A(H5) viruses in HA clade 2.3.4.4b and lacked amino acid changes that improve recognition of mammalian receptors or fusion of the viral membrane with the host endosomal membranes. (cdc.gov)
  • In contrast, the basic nitrogen causes repulsion in other PTPs containing an asparagine in the equivalent position resulting in a remarkable selectivity for PTP1B. (rcsb.org)
  • Electronegative atoms which often take part in hydrogen bonds are oxygen, nitrogen and fluorine (not present in amino acid side chains). (tu-muenchen.de)
  • within selection The respective amino acids were colored by element, s.t. oxygen is red, nitrogen is blue, hydrogen is white and sulfur is yellow. (tu-muenchen.de)
  • In the present study, we investigated whether a non-pathogenic H9N2 virus, A/chicken/Yokohama/aq-55/2001 (Y55) (H9N2), acquires pathogenicity in chickens when a pair of di-basic amino acid residues is introduced at the cleavage site of its HA molecule. (biomedcentral.com)
  • rgY55sub (H9N2), which had four basic amino acid residues at the HA cleavage site, replicated in MDCK cells in the absence of trypsin after six consecutive passages in the air sacs of chicks, and acquired intravenous pathogenicity to chicken after four additional passages. (biomedcentral.com)
  • On the other hand, an avirulent H5N1 strain, A/duck/Hokkaido/Vac-1/2004 (Vac1) (H5N1), acquired intranasal pathogenicity after a pair of di-basic amino acid residues was introduced into the cleavage site of the HA, followed by two passages by air sac inoculation in chicks. (biomedcentral.com)
  • Normal processing of amyloid precursor protein involves proteolytic cleavage at a site between residues Lys.sup.16 and Leu.sup.17 (as numbered for the .nu.AP region where Asp.sup.597 is residue 1 in Kang et al. (justia.com)
  • Comment: SMc02121 is quite similar and is the ATPase component of a putative amino acid transporter, so it is ignored. (lbl.gov)
  • Indicates the amino acid change of the variant. (expasy.org)
  • Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated. (expasy.org)
  • 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. (expasy.org)
  • The highly basic 55 amino acid nucleocapsid protein (NC) that coats the HIV-1 genome has two zinc fingers that differ by five amino acids (strain pNL4-3). (umd.edu)
  • 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. (lbl.gov)
  • Results show that amino acid differences at positions 24 and 27 contribute significantly to finger one's helix destabilizing activity and hence NC's chaperone activity. (umd.edu)
  • Our results showed that an amino acid substitution at position 185 in the V2 region of gp120 played a crucial role in regulating the b12 susceptibility of AE-Env-recombinant viruses by cooperating with 2 previously reported potential N-linked glycosylation (PNLG) sites at positions 186 (N186) and 197 (N197) in the V2 and C2 regions of Env gp120. (biomedcentral.com)
  • This structure permits ubiquitous proteases such as furin and PC6, which recognize multiple basic amino acids, to cleave the HA, leading to systemic infection in chickens. (biomedcentral.com)
  • The N terminus of mature rhodopsin is dually glycosylated at residues N2 and N15 ( Hargrave, 1977 ). (jneurosci.org)
  • Structurally, clovibactin featured two D-amino acids, d-alanine, and d-glutamic acid, in its four amino acid long linear N terminus and D-3-hydroxy asparagine, a unique amino acid residue. (news-medical.net)
  • secretase" at the amino-terminus of the .beta. (justia.com)
  • 1) Nucleic acids that can produce infectious forms of any of the select agent viruses listed in paragraph (b) of this section. (lawstack.com)
  • 4) A select agent or regulated nucleic acids that can produce infectious forms of any select agent virus that has been subjected to a validated inactivation procedure that is confirmed through a viability testing protocol. (lawstack.com)
  • 6) A select agent or regulated nucleic acids that can produce infectious forms of any select agent virus not subjected to a validated inactivation procedure or material containing a select agent not subjected to a procedure that removes all viable select agent cells, spores, or virus particles if the material is determined by the HHS Secretary to be effectively inactivated or effectively removed. (lawstack.com)
  • In previous A(H5N1) outbreaks and zoonosis the NA stalk region often had deletions (e.g., a 20 amino acid deletion at positions 49-68 relative to A/goose/Guangdong/1/1996) that enhances replication and/or pathogenesis in terrestrial poultry and mice ( 4-6 ). (cdc.gov)
  • The type 2 HP-PRRSV isolated in China in 2006 shows a unique discontinuous 30 amino acid deletion in the nonstructural protein 2 (nsp2) gene in open reading frame (ORF) 1a [ 5 , 7 ]. (biomedcentral.com)
  • Interestingly, we found that the standard strain in Japan, EDRD1, has a 39 amino acid deletion, which is in almost the same region as the nsp2 gene with the HP-PRRSV in the present study. (biomedcentral.com)
  • Particularly, in the extracellular domain, regions near the 70-amino acid island are known to be critical to BR binding. (biomedcentral.com)
  • In comparison, the exact function of the leucine rich-repeats (LRR) region located before the 70-amino acid island domain in the extracellular cellular portion of BRI1 has not yet been described, due to a lack of specific mutant alleles. (biomedcentral.com)
  • Our results indicated that the extracellular LRR regions before the 70-amino acid island domain of BRI1 are important for the appropriate cellular functioning of BRI1. (biomedcentral.com)
  • In the presence of BR, BKI1 is released by the direct binding of BR to the 70-amino acid island region in the extracellular domain of BRI1 [ 7 ]. (biomedcentral.com)
  • However, theoverall shape, the position of long loops, a conserved alpha-helix thatcovers the amino-terminal end of the parallel beta-helix and stacks ofresidues in alphaR-conformation at the start of PB1 all suggest a commonancestor. (embl.de)
  • Des X" = "an amino acid does not have to be present at this position. (lawstack.com)
  • To increase the utilization of current computational resources, we 﫿rst provide an overview of computational prediction of amino acid variations that influence protein PTMs and their functional analysis. (deepdyve.com)
  • PTMs are specific to types of amino acid residues. (deepdyve.com)
  • In this regard, comprehensive studies of the impact of amino acid variation on protein PTMs will be helpful for further understanding of how genetic polymorphisms are involved in regulating biological and pathological processes and providing instructive information for drug development of various related diseases. (deepdyve.com)
  • The amino acid variation S326C of human OGG1 disrupts Ser-326 phosphorylation site and affects susceptibility to a variety of cancers [9]. (deepdyve.com)
  • Conservation of asparagines might be connected with asparagine-ladders that contribute to the stability of the fold. (embl.de)
  • At the center of protein-protein interactions are the binding surfaces, or interfacial residues which form contacts between binding partners and stabilize protein complexes. (biomedcentral.com)
  • Wild-type-to-mutant titration experiments showed that the nonresponsive phenotype is dominant: A single nonresponsive residue within a pentameric receptor is sufficient to render the receptor nonresponsive. (nih.gov)
  • When MspA's residues are colored by charge (negatively charged amino acids are shown in red, positively charged in blue and neutral in gray) we can see that the native MspA protein might not let a negatively changed molecule like DNA pass through (see if you can see why). (scienceblogs.com)
  • Consequently, amino acid variations through changing the type of residues of the target sites or key flanking residues could directly or indirectly influence PTM of protein and bring about a detrimental effect on protein function. (deepdyve.com)
  • Although characteristically variable and postulated to be a flexible structure, the HVR1 has genetic constraints upon its amino acid composition. (biomedcentral.com)
  • Penin et al found that while the amino acid variability of the HVR1 in response to the immune pressure is extensive, the conformation and the physicochemical properties of the HVR1 were ultimately conserved [ 9 ]. (biomedcentral.com)
  • But figure 2 shows that the mutated amino acid is on the surface of the protein and therefore we have to take a look at the biophysical properties of the mutated and the wildtype sidechains. (tu-muenchen.de)