The Universal Statistical Distributions of the Affinity, Equilibrium Constants, Kinetics and Specificity in Biomolecular Recognition

	The Universal Statistical Distributions of the Affinity, Equilibrium Constants, Kinetics and Specificity in Biomolecular Recognition
	Zheng,Xiliang; Wang,Jin
刊名	plos computational biology
	2015
卷号	11 期号:4 页码:5493-5497
关键词	SINGLE-MOLECULE DYNAMICS RANDOM-ENERGY-MODEL PROTEIN-FOLDING FUNNELS 3-HELIX BUNDLE PROTEIN DRUG DISCOVERY COMBINATORIAL TECHNOLOGIES ENZYMATIC DYNAMICS INTERFACE BINDING LANDSCAPE MODEL LIGAND-BINDING
通讯作者	zheng,xl
英文摘要	we uncovered the universal statistical laws for the biomolecular recognition/binding process. we quantified the statistical energy landscapes for binding, from which we can characterize the distributions of the binding free energy (affinity), the equilibrium constants, the kinetics and the specificity by exploring the different ligands binding with a particular receptor. the results of the analytical studies are confirmed by the microscopic flexible docking simulations. the distribution of binding affinity is gaussian around the mean and becomes exponential near the tail. the equilibrium constants of the binding follow a log-normal distribution around the mean and a power law distribution in the tail. the intrinsic specificity for biomolecular recognition measures the degree of discrimination of native versus non-native binding and the optimization of which becomes the maximization of the ratio of the free energy gap between the native state and the average of non-native states versus the roughness measured by the variance of the free energy landscape around its mean. the intrinsic specificity obeys a gaussian distribution near the mean and an exponential distribution near the tail. furthermore, the kinetics of binding follows a log-normal distribution near the mean and a power law distribution at the tail. our study provides new insights into the statistical nature of thermodynamics, kinetics and function from different ligands binding with a specific receptor or equivalently specific ligand binding with different receptors. the elucidation of distributions of the kinetics and free energy has guiding roles in studying biomolecular recognition and function through small-molecule evolution and chemical genetics.
收录类别	SCI
语种	英语
WOS记录号	WOS:000354517600053
公开日期	2016-05-31
内容类型	期刊论文
源URL	[http://ir.ciac.jl.cn/handle/322003/65113]
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	Zheng,Xiliang,Wang,Jin. The Universal Statistical Distributions of the Affinity, Equilibrium Constants, Kinetics and Specificity in Biomolecular Recognition[J]. plos computational biology,2015,11(4):5493-5497.
APA	Zheng,Xiliang,&Wang,Jin.(2015).The Universal Statistical Distributions of the Affinity, Equilibrium Constants, Kinetics and Specificity in Biomolecular Recognition.plos computational biology,11(4),5493-5497.
MLA	Zheng,Xiliang,et al."The Universal Statistical Distributions of the Affinity, Equilibrium Constants, Kinetics and Specificity in Biomolecular Recognition".plos computational biology 11.4(2015):5493-5497.