Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
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Recent applications of Kirkwood-Buff theory to biological systemsBiomolecular electrostatics and solvation: a computational perspectiveFragment-based identification of determinants of conformational and spectroscopic change at the ricin active siteMannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motionsTime-resolved study of the inner space of lactose permeaseConformational stability of CopC and roles of residues Tyr79 and Trp83.The effect of metals on SDS-induced partially folded states of CopC.Salt-stabilized globular protein structure in 7 M aqueous urea solution.Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydrationMechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured then for the native protein.The effect of denaturants on protein structure.Orthophosphate anion enhances the stability and activity of endoxylanase from Bacillus sp.Backbone additivity in the transfer model of protein solvation.Different factors affecting human ANP amyloid aggregation and their implications in congestive heart failure.Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?Serge Timasheff: the man with a genius for solutions in biology.Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components.Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a two-domain modelProbing protein-sugar interactions.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.The molecular basis for the chemical denaturation of proteins by urea.Strategies to stabilize compact folding and minimize aggregation of antibody-based fragmentsA molecular mechanism for osmolyte-induced protein stabilityResurrecting Van Leeuwenhoek's rotifers: a reappraisal of the role of disaccharides in anhydrobiosis.The Energetics of Streptococcal Enolase Octamer Formation: The Quantitative Contributions of the Last Eight Amino Acids at the Carboxy-Terminus.Changes in solvation during DNA binding and cleavage are critical to altered specificity of the EcoRI endonucleaseOsmolyte-induced perturbations of hydrogen bonding between hydration layer waters: correlation with protein conformational changes.Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation.Urea-induced dissociation and unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric and spectral studies.On the role of surface tension in the stabilization of globular proteins.Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra.A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions.Phosphorylated tau can promote tubulin assembly.In disperse solution, "osmotic stress" is a restricted case of preferential interactions.Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor.Changes in water structure induced by the guanidinium cation and implications for protein denaturation.Differences in water release for the binding of EcoRI to specific and nonspecific DNA sequences.Glycerol-induced development of catalytically active conformation of Crotalus adamanteus L-amino acid oxidase in vitroFolding of RNA tertiary structure: Linkages between backbone phosphates, ions, and water.Effect of trehalose on amyloid beta (29-40)-membrane interaction.
P2860
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P2860
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
description
1992 nî lūn-bûn
@nan
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@ast
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@en
type
label
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@ast
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@en
prefLabel
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@ast
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@en
P356
P1433
P1476
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.
@en
P2093
Timasheff SN
P304
P356
10.1021/BI00156A001
P407
P577
1992-10-01T00:00:00Z