Assignment of 1H, 13C and 15N resonances of the a′ domain of protein disulfide isomerase

被引：20

作者：

Dijkstra, K

Karvonen, P

Pirneskoski, A

Koivunen, P

Kivirikko, KI

Darby, NJ

van Straaten, M

Scheek, RM

Kemmink, J

机构：

[1] European Mol Biol Lab, D-69012 Heidelberg, Germany

[2] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands

[3] Univ Oulu, Bioctr, Collagen Res Unit, FIN-90220 Oulu, Finland

[4] Univ Oulu, Dept Med Biochem, FIN-90220 Oulu, Finland

[5] Univ Oulu, Dept Biochem, FIN-90571 Oulu, Finland

[6] Univ Oulu, Bioctr, FIN-90571 Oulu, Finland

来源：

JOURNAL OF BIOMOLECULAR NMR | 1999年 / 14卷 / 02期

关键词：

disulfide bond; prolyl-4-hydroxylase; protein disulfide isomerase; protein folding; thioredoxin;

D O I：

10.1023/A:1008331225208

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：195 / 196

页数：2

共 10 条

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[9] The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
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[10] 2-DIMENSIONAL NMR EXPERIMENTS FOR CORRELATING C-13-BETA AND H-1-DELTA/EPSILON CHEMICAL-SHIFTS OF AROMATIC RESIDUES IN C-13-LABELED PROTEINS VIA SCALAR COUPLINGS
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