A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease.
about
Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model.Structured disorder and conformational selection.Destabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type.Effect of BET Missense Mutations on Bromodomain Function, Inhibitor Binding and Stability.Folding subdomains of thioredoxin characterized by native-state hydrogen exchangeThermodynamics of protein denatured states.Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.Heat capacity changes upon burial of polar and nonpolar groups in proteins.Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein.Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.The fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model.Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation.The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble.Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range.Folding of intracellular retinol and retinoic acid binding proteins.Glutamate counteracts the denaturing effect of urea through its effect on the denatured state.Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble.The Kirkwood-Buff theory and the effect of cosolvents on biochemical reactions.Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Conformational analysis and design of cross-strand disulfides in antiparallel β-sheets.
P2860
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P2860
A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
A model of the changes in dena ...... ts in staphylococcal nuclease.
@ast
A model of the changes in dena ...... ts in staphylococcal nuclease.
@en
type
label
A model of the changes in dena ...... ts in staphylococcal nuclease.
@ast
A model of the changes in dena ...... ts in staphylococcal nuclease.
@en
prefLabel
A model of the changes in dena ...... ts in staphylococcal nuclease.
@ast
A model of the changes in dena ...... ts in staphylococcal nuclease.
@en
P356
P1476
A model of the changes in dena ...... ts in staphylococcal nuclease.
@en
P2093
P2888
P304
P356
10.1038/12338
P577
1999-09-01T00:00:00Z
P6179
1039393746