Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants.
about
Porphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzymeStructurally homologous all beta-barrel proteins adopt different mechanisms of foldingEarly formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchangeThe effect of Glu75 of staphylococcal nuclease on enzyme activity, protein stability and protein unfolding.Thermodynamic effects of mutations on the denaturation of T4 lysozymeChemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption.Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease foldingPressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation"Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease.Coupling between trans/cis proline isomerization and protein stability in staphylococcal nucleaseThe kinetic basis for the stabilization of staphylococcal nuclease by xylose.Stochastic emergence of multiple intermediates detected by single-molecule quasi-static mechanical unfolding of protein.Biosynthetic incorporation of tryptophan analogues into staphylococcal nuclease: effect of 5-hydroxytryptophan and 7-azatryptophan on structure and stability.Rational stabilization of complex proteins: a divide and combine approach.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.Heat capacity change for ribonuclease A folding.The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.Domains in folding of model proteinsA stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes.Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.Mutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble.
P2860
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P2860
Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants.
description
1994 nî lūn-bûn
@nan
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@ast
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@en
type
label
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@ast
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@en
prefLabel
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@ast
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@en
P2093
P356
P1433
P1476
Three-state thermodynamic anal ...... aphylococcal nuclease mutants.
@en
P2093
Anderson EA
Privalov PL
P304
10842-10850
P356
10.1021/BI00201A035
P407
P577
1994-09-01T00:00:00Z