Two exposed amino acid residues confer thermostability on a cold shock protein
about
Shewanella spp. genomic evolution for a cold marine lifestyle and in-situ explosive biodegradationThe cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factorRole of conserved salt bridges in homeodomain stability and DNA bindingNative protein sequences are close to optimal for their structuresMutation of exposed hydrophobic amino acids to arginine to increase protein stabilityEmerging role of N- and C-terminal interactions in stabilizing (β/α)8 fold with special emphasis on Family 10 xylanasesSelected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpartSolution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritimaThe crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridgesIncreasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop.Positive contribution of hydration structure on the surface of human lysozyme to the conformational stabilityKinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surfaceComparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stabilitySolution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeonThermococcus celerAn Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants from Alicyclobacillus acidocaldariusSolution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet foldCorticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered releaseCrystal structure of a cold-adapted class C beta-lactamaseEngineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structureStructural Insights into the Specificity of Xyn10B from Paenibacillus barcinonensis and Its Improved Stability by Forced Protein EvolutionA Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature ActivitySolution structure of the cold-shock-like protein fromRickettsia rickettsiiThermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architectureStructure of a thermophilic cyanobacterial b6f-type Rieske proteinRapid Bioinformatic Identification of Thermostabilizing MutationsRemoval of surface charge-charge interactions from ubiquitin leaves the protein folded and very stableThe critical role of partially exposed N-terminal valine residue in stabilizing GH10 xylanase from Bacillus sp.NG-27 under poly-extreme conditionsUnusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulationsA double-deletion method to quantifying incremental binding energies in proteins from experiment: example of a destabilizing hydrogen bonding pair.Electrostatic contributions to the kinetics and thermodynamics of protein assemblyGlucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamicsThermal adaptation of α-amylases: a review.Biochemical characterization of a beta-galactosidase with a low temperature optimum obtained from an Antarctic arthrobacter isolate.Distance dependence and salt sensitivity of pairwise, coulombic interactions in a proteinInferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions.Thermostability in endoglucanases is fold-specificProtein threading by learning.Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.
P2860
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P2860
Two exposed amino acid residues confer thermostability on a cold shock protein
description
2000 nî lūn-bûn
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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Two exposed amino acid residues confer thermostability on a cold shock protein
@ast
Two exposed amino acid residues confer thermostability on a cold shock protein
@en
Two exposed amino acid residues confer thermostability on a cold shock protein
@nl
type
label
Two exposed amino acid residues confer thermostability on a cold shock protein
@ast
Two exposed amino acid residues confer thermostability on a cold shock protein
@en
Two exposed amino acid residues confer thermostability on a cold shock protein
@nl
prefLabel
Two exposed amino acid residues confer thermostability on a cold shock protein
@ast
Two exposed amino acid residues confer thermostability on a cold shock protein
@en
Two exposed amino acid residues confer thermostability on a cold shock protein
@nl
P2093
P356
P1476
Two exposed amino acid residues confer thermostability on a cold shock protein
@en
P2093
P356
10.1038/75151
P407
P577
2000-05-01T00:00:00Z