Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.
about
Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases.Cytochrome c folds through a smooth funnelAlleviation of a defect in protein folding by increasing the rate of subunit assembly.Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.
P2860
Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Refolding rate of stability-en ...... f thermodynamic driving force.
@ast
Refolding rate of stability-en ...... f thermodynamic driving force.
@en
type
label
Refolding rate of stability-en ...... f thermodynamic driving force.
@ast
Refolding rate of stability-en ...... f thermodynamic driving force.
@en
prefLabel
Refolding rate of stability-en ...... f thermodynamic driving force.
@ast
Refolding rate of stability-en ...... f thermodynamic driving force.
@en
P2860
P356
P1433
P1476
Refolding rate of stability-en ...... f thermodynamic driving force.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560070501
P577
1998-05-01T00:00:00Z