Nuclear magnetic resonance studies of redox-induced conformational changes in thioredoxin from Escherichia coli.
about
Thioredoxin A Active-Site Mutants Form Mixed Disulfide Dimers That Resemble Enzyme–Substrate Reaction IntermediatesStructure of human thioredoxin exhibits a large conformational changeNucleotide sequence and protein overproduction of bacteriophage T4 thioredoxin.Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein.Conformational and functional similarities between glutaredoxin and thioredoxins.Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional 1H NMR spectroscopy.
P2860
Nuclear magnetic resonance studies of redox-induced conformational changes in thioredoxin from Escherichia coli.
description
1976 nî lūn-bûn
@nan
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
1976年论文
@zh
1976年论文
@zh-cn
name
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@en
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@nl
type
label
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@en
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@nl
prefLabel
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@en
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@nl
P2860
P1433
P1476
Nuclear magnetic resonance stu ...... redoxin from Escherichia coli.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(76)80946-5
P407
P577
1976-12-01T00:00:00Z