Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics

	Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
	Lu Q ; Lu HP ; Wang J
刊名	physical review letters
	2007
卷号	98 期号:12 页码:文献编号：128105
关键词	ALDRICH-SYNDROME PROTEIN TRANSITION-STATE CONFORMATIONAL DYNAMICS CDC42 BINDING DETERMINES LANDSCAPES DOMAIN
ISSN号	0031-9007
通讯作者	lu q
中文摘要	combining a single-molecule study of protein binding with a coarse grained molecular dynamics model including solvent (water molecules) effects, we find that biomolecular recognition is determined by flexibilities in addition to structures. our single-molecule study shows that binding of cbd (a fragment of wiskott-aldrich syndrome protein) to cdc42 involves bound and loosely bound states, which can be quantitatively explained in our model as a result of binding with large conformational changes. our model identified certain key residues for binding consistent with mutational experiments. our study reveals the role of flexibility and a new scenario of dimeric binding between the monomers: first bind and then fold.
收录类别	SCI
语种	英语
公开日期	2010-07-13 ; 2011-06-09
内容类型	期刊论文
源URL	[http://ir.ciac.jl.cn/handle/322003/14027]
专题	长春应用化学研究所_长春应用化学研究所知识产出_期刊论文
推荐引用方式 GB/T 7714	Lu Q,Lu HP,Wang J. Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics[J]. physical review letters,2007,98(12):文献编号：128105.
APA	Lu Q,Lu HP,&Wang J.(2007).Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics.physical review letters,98(12),文献编号：128105.
MLA	Lu Q,et al."Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics".physical review letters 98.12(2007):文献编号：128105.