1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states

被引：13

作者：

Hsu, Shang-Te Danny ^{[1
]}

Cabrita, Lisa D. ^{[1
,2
,3
]}

Christodoulou, John ^{[1
,2
,3
]}

Dobson, Christopher M. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] Univ London, Inst Struct & Mol Biol, Res Dept Struct & Mol Biol, London, England

[3] Univ London, Birkbeck Coll, Sch Crystallog, London, England

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2009年 / 3卷 / 01期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

Protein folding; Nascent chain; Urea; Ribosome; ABP-120; NMR; FILAMINS; ROD;

D O I：

10.1007/s12104-008-9134-4

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The gelation factor from Dictyostelium discoideum (ABP-120) is an actin binding protein consisting of six immunoglobulin (Ig) domains in the C-terminal rod domain. We have recently used the pair of domains 5 and 6 of ABP-120 as a model system for studying multi-domain nascent chain folding on the ribosome. Here we present the NMR assignments of domain 5 in its native and 8M urea-denatured states.

引用

页码：29 / 31

页数：3

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