Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes.
about
Residual structure in unfolded proteinsUrea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsThe effect of chemical chaperones on the assembly and stability of HIV-1 capsid proteinPhysical-chemical determinants of coil conformations in globular proteins.Toward an atomistic description of the urea-denatured state of proteins.Probing osmolyte participation in the unfolding transition state of a protein.Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domainsQuantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationSynergy in protein-osmolyte mixtures.Beneficial effect of sugar osmolytes on the refolding of guanidine hydrochloride-denatured trehalose-6-phosphate hydrolase from Bacillus licheniformis.Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityProperties of hydrophobic free energy found by gas-liquid transferAllosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Urea-temperature phase diagrams capture the thermodynamics of denatured state expansion that accompany protein unfolding.How, when and why proteins collapse: the relation to folding.The new view of hydrophobic free energy.Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains.Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Untangling a Structurally Resolved Protein Folding IntermediateDry molten globule intermediates and the mechanism of protein unfolding.Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.In vivo detection and quantification of chemicals that enhance protein stability.Counting peptide-water hydrogen bonds in unfolded proteins.Chemical chaperones assist intracellular folding to buffer mutational variations.The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.The effect of urea on aqueous hydrophobic contact-pair interactions.Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein."Cooperative collapse" of the denatured state revealed through Clausius-Clapeyron analysis of protein denaturation phase diagrams.Modulation of the Thermodynamic Signatures of an RNA Thermometer by Osmolytes and Salts.
P2860
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P2860
Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@en
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@nl
type
label
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@en
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@nl
prefLabel
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@en
Hydrogen bonding progressively ...... ater and protecting osmolytes.
@nl
P2860
P356
P1433
P1476
Hydrogen bonding progressively ...... water and protecting osmolytes
@en
P2093
D Wayne Bolen
Luis Marcelo F Holthauzen
P2860
P304
P356
10.1021/BI9015499
P407
P50
P577
2010-02-01T00:00:00Z