Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.
about
NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase.The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling.The Sec System: Protein Export in Escherichia coli.
P2860
Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@en
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@nl
type
label
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@en
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@nl
prefLabel
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@en
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@nl
P2093
P2860
P356
P1476
Electron spin resonance and fl ...... bstrate to the chaperone SecB.
@en
P2093
P2860
P304
33681-33688
P356
10.1074/JBC.M104466200
P407
P577
2001-07-02T00:00:00Z