The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state.
about
Inhibitor and substrate binding induced stability of HIV-1 protease against sequential dissociation and unfolding revealed by high pressure spectroscopy and kineticsInvestigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.Predicting protein folding cores by empirical potential functions.Destabilizing mutations alter the hydrogen exchange mechanism in ribonuclease A.How general is the nucleation-condensation mechanism?
P2860
The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
The contribution of the residu ...... sure-folding transition state.
@en
The contribution of the residu ...... sure-folding transition state.
@nl
type
label
The contribution of the residu ...... sure-folding transition state.
@en
The contribution of the residu ...... sure-folding transition state.
@nl
prefLabel
The contribution of the residu ...... sure-folding transition state.
@en
The contribution of the residu ...... sure-folding transition state.
@nl
P2860
P50
P356
P1433
P1476
The contribution of the residu ...... ssure-folding transition state
@en
P2093
Josep Font
Reinhard Lange
P2860
P304
P356
10.1110/PS.052050306
P577
2006-04-05T00:00:00Z