• amino acids
  • Coexistence of amine solutes, typically diamines, polyamines, amino acid esters, and amidated amino acids decreases the heat-induced inactivation rate of proteins by one order of magnitude compared with that in the absence of additives under low concentrations of proteins at physiological pH. (eurekaselect.com)
  • Due to the numerous ionizable side chains of amino acids found throughout a protein, the pH at which a protein is placed is crucial to its stability. (wikipedia.org)
  • Hofmeister was the first to propose that polypeptides were amino acids linked by peptide bonds in 1902, although this model of protein primary structure was independently and simultaneously conceived by Emil Fischer. (wikipedia.org)
  • Hofmeister also argued for peptide bonds based on the biuret reaction observed with all proteins but never with free amino acids. (wikipedia.org)
  • KMT2D is a large protein over 5,500 amino acids in size and is widely expressed in adult tissues. (wikipedia.org)
  • The mouse and human KMT2D proteins are 5,588 and 5,537 amino acids in length, respectively. (wikipedia.org)
  • Each protein exists as an unfolded polypeptide or random coil when translated from a sequence of mRNA to a linear chain of amino acids. (wikipedia.org)
  • Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), known as the native state. (wikipedia.org)
  • Preventing this calcium from originally binding to the molecule by mutation of its binding site, reduced thermolysin stability by 7 °C. However, while calcium binding makes a significant contribution to stabilising thermolysin, more crucial to stability is a small cluster of N-terminal domain amino acids located at the proteins surface. (wikipedia.org)
  • Changing these amino acids to threonine (T) and alanine (A) respectively in a less stable thermolysin-like proteinase produced by Bacillus stearothermophillus (TLP-ste), results in individual reductions in stability of 7 °C (F63→T) and 6.3 °C (P69→A) and when combined a reduction in stability of 12.3 °C. In the synthesis of aspartame, less bitter-tasting byproduct is produced when the reaction is catalyzed by thermolysin. (wikipedia.org)
  • The PAK4 generates 12 transcripts of which 10 coding transcripts are predicted to code proteins of about 438 to 591 amino acids long, while remaining two transcripts are non-coding in nature. (wikipedia.org)
  • molecules
  • The development of the use of proteins, especially monoclonal antibodies (mAbs), as therapeutic molecules has provided many challenges. (selectscience.net)
  • The net contribution of an intramolecular hydrogen bond, an intermolecular one between protein and ordered water molecules, and an intermolecular one between ordered water molecules was estimated to be 8.5, 5.2, and 5.0 kJ/mol, respectively, for a hydrogen bond with 3 Å length. (nii.ac.jp)
  • The phenomenon of macromolecular crowding alters the properties of molecules in a solution when high concentrations of macromolecules such as proteins are present. (wikipedia.org)
  • aqueous
  • The denaturing of proteins by an aqueous solution containing many types of ions is more complicated as all the ions can act, according to their Hofmeister activity, i.e., a fractional number specifying the position of the ion in the series (given previously) in terms of its relative efficiency in denaturing a reference protein. (wikipedia.org)
  • Sequence
  • One of the reasons is that a protein structure is prescribed not only by a part of the amino acid sequence but also by an extensive interaction. (nii.ac.jp)
  • The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. (wikipedia.org)
  • The essential fact of folding, however, remains that the amino acid sequence of each protein contains the information that specifies both the native structure and the pathway to attain that state. (wikipedia.org)
  • DNA: 5' - AAC AGC CTG CGT ACG GCT CTC - 3' 3' - TTG TCG GAC GCA TGC CGA GAG - 5' mRNA: 5' - AAC AGC CUG CGU ACG GCU CUC - 3' Protein: Asn Ser Leu Arg Thr Ala Leu LMNA missense mutation (c.1580G>T) introduced at LMNA gene - position 1580 (nt) in the DNA sequence (CGT) causing the guanine to be replaced with the thymine, yielding CTT in the DNA sequence. (wikipedia.org)
  • functional
  • Hello everyone, After purifying a membrane protein, how do you know if it's stable or functional. (protocol-online.org)
  • Conformational stability is athermodynamic quantity which refl ects the populationof protein in its native, functional state. (teknoscienze.com)
  • It is likely that both protein context (location of the BRCT domains at the C-terminus of the large BRCA1 protein) and cellular environment (binding partners, molecular chaperones) buffer these destabilizing effects such that at least some mutant protein is able to adopt the folded functional state. (sigmaaldrich.com)
  • The SMN2 gene, on the other hand - due to a variation in a single nucleotide (840.C→T) - undergoes alternative splicing at the junction of intron 6 to exon 8, with only 10-20% of SMN2 transcripts coding a fully functional survival of motor neuron protein (SMN-fl) and 80-90% of transcripts resulting in a truncated protein compound (SMNΔ7) which is rapidly degraded in the cell. (wikipedia.org)
  • Almost all people, however, have at least one functional copy of the SMN2 gene (with most having 2-4 of them) which still codes small amounts of SMN protein - around 10-20% of the normal level - allowing some neurons to survive. (wikipedia.org)
  • Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. (wikipedia.org)
  • The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, so that protein dynamics is important. (wikipedia.org)
  • in other words, multiple polypeptide chains could interact to form a fully functional quaternary protein. (wikipedia.org)
  • effector
  • In addition to other mechanisms, PAK4 functions are mediated though phosphorylation of its effector proteins, including, LIMK1-Thr508, integrin β5-Ser759/Ser762, p120-catenin-Ser288, superior cervical ganglia 10 (SCG10)-Ser50, GEF-H1-Ser810 β-catenin-Ser675, and Smad2-Ser465. (wikipedia.org)
  • peptide
  • Accurate peptide ID is fundamental to accurate protein quantitation and post-translational modification (PTM) analysis. (technologynetworks.com)
  • However, these salts also interact directly with proteins (which are charged and have strong dipole moments) and may even bind specifically (e.g., phosphate and sulfate binding to ribonuclease A). Ions that have a strong salting in effect such as I− and SCN− are strong denaturants, because they salt in the peptide group, and thus interact much more strongly with the unfolded form of a protein than with its native form. (wikipedia.org)
  • Since biuret has the formula NH2-CO-NH-CO-NH2, that suggested the presence of similar peptide bonds in proteins. (wikipedia.org)
  • binds
  • The protein selectively binds enhancer regions based on type of cell and stage of differentiation. (wikipedia.org)
  • Structural analysis has shown that PUMA directly binds to antiapoptotic Bcl-2 family proteins via an amphiphatic α-helical structure which is formed by the BH3 domain. (wikipedia.org)
  • Contribution
  • In order to estimate the contribution of each factor to protein stability, the data of structure and stability changes must be expanded by studying many mutant proteins with systematic and comprehensive substitutions. (nii.ac.jp)
  • Contribution of Intra- and Intermolecular Hygrogen Bonds to the Conformational Stability of Human Lysozyme'Biochemistry. (nii.ac.jp)
  • Contribution of Amino Acid Substitutions at Two Different Interior Positions to the Stability of Human Lysozyme'Protein Engineering. (nii.ac.jp)
  • Using a mutated pseudo-wild-type protein specifically mutated to prevent precipitation at high pH, the salt bridge's contribution to the overall free energy of the folded protein state can be determined by performing a point-mutation, altering and, consequently, breaking the salt bridge. (wikipedia.org)
  • Formation of intramolecular hydrogen bonds provides another important contribution to protein stability. (wikipedia.org)
  • Studies on the contribution of calcium to thermolysin stability have shown that upon thermal inactivation a single calcium ion is released from the molecule. (wikipedia.org)
  • contrast
  • By contrast, the mutation R1699L, which disrupts the binding of phosphorylated proteins (but which is not destabilizing), was completely inactive. (sigmaaldrich.com)
  • concentrations
  • When separating proteins or small nucleic acids (DNA, RNA, or oligonucleotides) the gel is usually composed of different concentrations of acrylamide and a cross-linker, producing different sized mesh networks of polyacrylamide. (wikipedia.org)
  • accumulation
  • In Fragile X syndrome-a genetic mishap that results in cognitive delays-the lack of a translation-repressing protein leads to the rampant accumulation of other proteins in the mouse brain. (the-scientist.com)
  • Determining
  • The protein co-localizes with lineage determining transcription factors on transcriptional enhancers and is essential for cell differentiation and embryonic development. (wikipedia.org)
  • Determining protein stability in cell lysate using the fast parallel proteolysis (FASTpp) assay. (wikipedia.org)
  • sequences
  • Understanding how tertiary structures of proteins are coded for in their amino acid sequences is one of the main targets in modern life science research. (nii.ac.jp)
  • secretion
  • This domain is found among distantly related species from the six kingdoms: Eubacteria, Archaebacteria, Protista, Fungi, Plantae, and Animalia and is known to be involved in Golgi organization and protein secretion. (wikipedia.org)
  • stable
  • These results indicate that the primary effect of the stu1-5 mutation is to make the protein less stable. (genetics.org)
  • crucial
  • Download this free white paper from Protein Simple to learn about the differences between MFI and how MFI provides crucial information about your protein therapeutic. (technologynetworks.com)
  • In healthy individuals, the SMN1 gene codes the survival of motor neuron protein (SMN) which, as its name says, plays a crucial role in survival of motor neurons. (wikipedia.org)
  • conformational changes
  • It has also been shown that macromolecular crowding affects protein-folding dynamics as well as overall protein shape where distinct conformational changes are accompanied by secondary structure alterations implying that crowding-induced shape changes may be important for protein function and malfunction in vivo. (wikipedia.org)
  • mutant
  • A proteasomal mutation was found to suppress the faf mutant phenotype, suggesting that FAF protein has activity that antagonizes proteasome function. (genetics.org)
  • In this project, we tried to estimate some factors that contribute to conformational stability of a protein using data base of stability/structure, which are obtained from a series of mutant human lysozymes. (nii.ac.jp)
  • Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozyme'Protein Engineering. (nii.ac.jp)
  • function
  • Lower levels of the protein results in loss of function of neuronal cells in the anterior horn of the spinal cord and subsequent system-wide atrophy of skeletal muscles. (wikipedia.org)
  • Proteins: Structure, Function, and Bioinformatics. (wikipedia.org)
  • Alternatively, the amino acid substitution could occur in a region of the protein which does not significantly affect the protein secondary structure or function. (wikipedia.org)
  • purification
  • Repeated crystallization was a favourite purification technique in the early days of protein science, and was essential for its development. (wikipedia.org)
  • sufficiently
  • Thus, the 6th amino acid glutamic acid is substituted by valine-notated as an "E6V" mutation-and the protein is sufficiently altered to cause the sickle-cell disease. (wikipedia.org)
  • inactivation
  • The amine compounds mainly suppress chemical modification, typically the β-elimination of disulfide bond and deamidation of asparagine side chain, thereby preventing heat-induced inactivation of proteins. (eurekaselect.com)
  • Amine compounds will be a key to prevent protein inactivation in solution additives. (eurekaselect.com)
  • gene
  • The disorder is caused by a genetic defect in the SMN1 gene, which encodes SMN, a protein widely expressed in all eukaryotic (ex: human) cells and necessary for survival of motor neurons. (wikipedia.org)
  • Transport and golgi organization 2 homolog (TANGO2) also known as chromosome 22 open reading frame 25 (C22orf25) is a protein that in humans is encoded by the TANGO2 gene. (wikipedia.org)
  • Mechanistically, KMT2C and KMT2D are required for the binding of H3K27 acetyltransferases CREB-binding protein (CBP) and/or p300 on enhancers, enhancer activation, and enhancer-promotor looping prior to gene transcription. (wikipedia.org)
  • Guanine nucleotide-binding protein-like 3, also known as nucleostemin, is a protein that in humans is encoded by the GNL3 gene. (wikipedia.org)
  • In humans, the Bcl-2-binding component 3 protein is encoded by the BBC3 gene. (wikipedia.org)
  • proteasome
  • Ubiquitinated proteins are targeted to the 26S proteasome, which consists of the 19S particle and the 20S proteasome (reviewed in G lickman 2000 ). (genetics.org)
  • The unfolded and extended polypeptides are then allowed to enter the rings of the 20S proteasome, the proteolytic core that contains multiple peptidase activities for protein degradation. (genetics.org)
  • substitution
  • Missense mutation or substitution refers to a change in one amino acid in a protein, arising from a point mutation in a single nucleotide. (wikipedia.org)
  • Another type of nonsynonymous substitution is a nonsense mutation in which a codon is changed to a premature stop codon that results in truncation of the resulting protein. (wikipedia.org)