盘基网柄菌凝凝胶因子（ABP - 120）结构域5在天然状态和8M尿素变性状态下的1H、15N和13C归属
1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states.
作者信息
Hsu Shang-Te Danny, Cabrita Lisa D, Christodoulou John, Dobson Christopher M
机构信息
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom.
出版信息
Biomol NMR Assign. 2009 Jun;3(1):29-31. doi: 10.1007/s12104-008-9134-4. Epub 2008 Dec 18.
PMID:19636940
Abstract
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.
摘要
盘基网柄菌的凝胶化因子（ABP-120）是一种肌动蛋白结合蛋白，其C端杆状结构域由六个免疫球蛋白（Ig）结构域组成。我们最近将ABP-120的结构域5和6作为研究核糖体上多结构域新生链折叠的模型系统。本文展示了结构域5在天然状态和8M尿素变性状态下的核磁共振（NMR）归属。
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