title: Physicochemical bases for protein folding, dynamics, and protein-ligand binding.
abstract: Proteins are essential parts of living organisms and participate in virtually every process within cells. As the genomic sequences for increasing number of organisms are completed, research into how proteins can perform such a variety of functions has become much more intensive because the value of the genomic sequences relies on the accuracy of understanding the encoded gene products. Although the static three-dimensional structures of many proteins are known, the functions of proteins are ultimately governed by their dynamic characteristics, including the folding process, conformational fluctuations, molecular motions, and protein-ligand interactions. In this review, the physicochemical principles underlying these dynamic processes are discussed in depth based on the free energy landscape (FEL) theory. Questions of why and how proteins fold into their native conformational states, why proteins are inherently dynamic, and how their dynamic personalities govern protein functions are answered. This paper will contribute to the understanding of structure-function relationship of proteins in the post-genome era of life science research.
authors.affiliation: School of Mathematics and Computer Science, Yunnan University of Nationalities, Kunming, 650500, China.|Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of Ministry of Education, Yunnan University, Kunming, 650091, China.
authors.forename: HuiMin
authors.initials: H
authors.lastname: Li
authors.affiliation: Teaching and Research Section of Computer, Department of Basic Medical, Kunming Medical University, Kunming, 650031, China.|Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of Ministry of Education, Yunnan University, Kunming, 650091, China.
authors.forename: YueHui
authors.initials: Y
authors.lastname: Xie
authors.affiliation: Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of Ministry of Education, Yunnan University, Kunming, 650091, China.|Southwest Biological Diversity Laboratory, Kunming Branch of Chinese Academy of Sciences, Kunming, 650223, China.
authors.forename: CiQuan
authors.initials: C
authors.lastname: Liu
authors.affiliation: Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of Ministry of Education, Yunnan University, Kunming, 650091, China. shuqunliu@gmail.com.|Southwest Biological Diversity Laboratory, Kunming Branch of Chinese Academy of Sciences, Kunming, 650223, China. shuqunliu@gmail.com.|Key Laboratory for Animal Genetic Diversity and Evolution of High Education in Yunnan Province, Kunming, 650091, China. shuqunliu@gmail.com.
authors.forename: ShuQun
authors.initials: S
authors.lastname: Liu
mesh_terms: D018360:Crystallography, X-Ray; D057927:Hydrophobic and Hydrophilic Interactions; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins