An analysis of the molecular origin of osmolyte-dependent protein stability
about
Occurrence of mitochondria-targeted Late Embryogenesis Abundant (LEA) gene in animals increases organelle resistance to water stressRecent applications of Kirkwood-Buff theory to biological systemsBiomolecular electrostatics and solvation: a computational perspectiveInteracting ions in biophysics: real is not idealThe influence of chemical chaperones on enzymatic activity under thermal and chemical stresses: common features and variation among diverse chemical familiesIdentifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.Glucosylglycerol and glucosylglycerate as enzyme stabilizers.Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin.Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.Crowding alone cannot account for cosolute effect on amyloid aggregationKirkwood-Buff integrals for ideal solutions.Identifying core features of adaptive metabolic mechanisms for chronic heat stress attenuation contributing to systems robustness.Liquid-vapor interfacial properties of aqueous solutions of guanidinium and methyl guanidinium chloride: influence of molecular orientation on interface fluctuations.Synergy in protein-osmolyte mixtures.Fluctuation theory of molecular association and conformational equilibria.Urea orientation at protein surfaces.Simulation study of ion pairing in concentrated aqueous salt solutions with a polarizable force fieldMacromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxinDistinctive solvation patterns make renal osmolytes diverse.Kirkwood-Buff theory of molecular and protein association, aggregation, and cellular crowdingOsmolyte solutions and protein folding.Thermodynamic and structural basis for relaxation of specificity in protein-DNA recognitionThe properties of residual water molecules in ionic liquids: a comparison between direct and inverse Kirkwood-Buff approaches.Inhibition of insulin fibrillation by osmolytes: Mechanistic insights.Volume exclusion and H-bonding dominate the thermodynamics and solvation of trimethylamine-N-oxide in aqueous urea.An osmolyte mitigates the destabilizing effect of protein crowding.How do thermophilic proteins resist aggregation?Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study.Aqueous ionic liquids and their influence on peptide conformations: denaturation and dehydration mechanisms.Putting the Piezolyte Hypothesis under Pressure.Aqueous ionic liquids in comparison with standard co-solutes : Differences and common principles in their interaction with protein and DNA structures.
P2860
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P2860
An analysis of the molecular origin of osmolyte-dependent protein stability
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
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2007年學術文章
@zh-hant
name
An analysis of the molecular origin of osmolyte-dependent protein stability
@en
An analysis of the molecular origin of osmolyte-dependent protein stability
@nl
type
label
An analysis of the molecular origin of osmolyte-dependent protein stability
@en
An analysis of the molecular origin of osmolyte-dependent protein stability
@nl
prefLabel
An analysis of the molecular origin of osmolyte-dependent protein stability
@en
An analysis of the molecular origin of osmolyte-dependent protein stability
@nl
P2093
P2860
P356
P1433
P1476
An analysis of the molecular origin of osmolyte-dependent protein stability
@en
P2093
B Montgomery Pettitt
David Wayne Bolen
Jörg Rösgen
P2860
P304
P356
10.1110/PS.062671607
P577
2007-02-27T00:00:00Z