Protein stability in mixed solvents: a balance of contact interaction and excluded volume
about
Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of anotherRecent applications of Kirkwood-Buff theory to biological systemsNovel determinants of the neuronal Cl(-) concentrationQuantifying the molecular origins of opposite solvent effects on protein-protein interactionsProtein Stabilization and the Hofmeister Effect: The Role of Hydrophobic SolvationStructural Basis for the Aminoacid Composition of Proteins from Halophilic ArcheaUrea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsThe osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.L-Arginine increases the solubility of unfolded species of hen egg white lysozyme.Effects of sucrose on the internal dynamics of azurin.Anion modulation of the 1H/2H exchange rates in backbone amide protons monitored by NMR spectroscopyUrea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.Interaction-component analysis of the hydration and urea effects on cytochrome c.Sodium perchlorate effects on the helical stability of a mainly alanine peptide.Proteins in binary solventsFlexibility of the cytoplasmic domain of the phototaxis transducer II from Natronomonas pharaonis.Soft interactions and crowding.Predicting the energetics of osmolyte-induced protein folding/unfolding.Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocolsOsmotic virial coefficients for model protein and colloidal solutions: importance of ensemble constraints in the analysis of light scattering data.Compensating effects of urea and trimethylamine-N-oxide on the heteroassociation of α-chymotrypsin and soybean trypsin inhibitorA contribution to the theory of preferential interaction coefficients.Stabilization of the predominant disease-causing aldolase variant (A149P) with zwitterionic osmolytesThe inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding proteinSynergy in protein-osmolyte mixtures.Coil-globule transition in the denatured state of a small proteinToward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditionsMacromolecular crowding fails to fold a globular protein in cellsA molecular mechanism for osmolyte-induced protein stabilityAnion currents in yeast K+ transporters (TRK) characterize a structural homologue of ligand-gated ion channels.On methods for determining solvent accessible surface area for proteins in their unfolded stateHalophilic enzyme activation induced by salts.Separating chemical and excluded volume interactions of polyethylene glycols with native proteins: Comparison with PEG effects on DNA helix formation.Anatomy of energetic changes accompanying urea-induced protein denaturation.Site-specific hydration dynamics of globular proteins and the role of constrained water in solvent exchange with amphiphilic cosolvents.Effects of Hofmeister anions on the phase transition temperature of elastin-like polypeptidesAssessing the solvent-dependent surface area of unfolded proteins using an ensemble modelIn silico Evaluation of Crosslinking Effects on Denaturant m(eq) values and ΔCp upon Protein UnfoldingProtein Stabilization and Enzyme Activation in Ionic Liquids: Specific Ion EffectsEffects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model
P2860
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P2860
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@ast
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@en
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@nl
type
label
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@ast
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@en
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@nl
prefLabel
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@ast
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@en
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@nl
P2860
P1433
P1476
Protein stability in mixed solvents: a balance of contact interaction and excluded volume
@en
P2093
John A Schellman
P2860
P304
P356
10.1016/S0006-3495(03)74459-2
P407
P577
2003-07-01T00:00:00Z