Predicting the energetics of osmolyte-induced protein folding/unfolding.
about
Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of anotherRecent applications of Kirkwood-Buff theory to biological systemsA backbone-based theory of protein foldingNMR structure of the viral peptide linked to the genome (VPg) of poliovirusThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPProtein Stabilization and the Hofmeister Effect: The Role of Hydrophobic SolvationThe influence of chemical chaperones on enzymatic activity under thermal and chemical stresses: common features and variation among diverse chemical familiesEntropic stabilization of proteins by TMAOThe osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Lactate dehydrogenase undergoes a substantial structural change to bind its substrateAnion modulation of the 1H/2H exchange rates in backbone amide protons monitored by NMR spectroscopyEffect of trehalose on protein structureUrea, 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.Protein folding at single-molecule resolution.Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)A hypothesis to reconcile the physical and chemical unfolding of proteins.Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.High-pressure SAXS study of folded and unfolded ensembles of proteinsAn overview of the importance of conformational flexibility in gene regulation by the transcription factors.Disordered allostery: lessons from glucocorticoid receptor.Crowding alone cannot account for cosolute effect on amyloid aggregationBackbone additivity in the transfer model of protein solvation.Probing osmolyte participation in the unfolding transition state of a protein.Cyclohexanehexol inhibitors of Abeta aggregation prevent and reverse Alzheimer phenotype in a mouse model.From the test tube to the cell: exploring the folding and aggregation of a beta-clam protein.Volume exclusion and soft interaction effects on protein stability under crowded conditions.Therapeutic protein aggregation: mechanisms, design, and control.Crowding and function reunitePolymer collapse in miscible good solvents is a generic phenomenon driven by preferential adsorption.Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domainsThe osmolyte TMAO stabilizes native RNA tertiary structures in the absence of Mg2+: evidence for a large barrier to folding from phosphate dehydration.Stabilization of the predominant disease-causing aldolase variant (A149P) with zwitterionic osmolytesBackbone and side-chain contributions in protein denaturation by urea.Protein denaturants at aqueous-hydrophobic interfaces: self-consistent correlation between induced interfacial fluctuations and denaturant stability at the interface.Synergy in protein-osmolyte mixtures.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Coil-globule transition in the denatured state of a small proteinToward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions
P2860
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P2860
Predicting the energetics of osmolyte-induced protein folding/unfolding.
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@ast
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@en
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@nl
type
label
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@ast
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@en
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@nl
prefLabel
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@ast
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@en
Predicting the energetics of osmolyte-induced protein folding/unfolding.
@nl
P2860
P356
P1476
Predicting the energetics of osmolyte-induced protein folding/unfolding
@en
P2093
D Wayne Bolen
P2860
P304
15065-15068
P356
10.1073/PNAS.0507053102
P407
P50
P577
2005-10-07T00:00:00Z