title: Predicting protein folding cores by empirical potential functions.
abstract: Theoretical and in vitro experiments suggest that protein folding cores form early in the process of folding, and that proteins may have evolved to optimize both folding speed and native-state stability. In our previous work (Chen et al., Structure, 14 (2006) 1401), we developed a set of empirical potential functions and used them to analyze interaction energies among secondary-structure elements in two beta-sandwich proteins. Our work on this group of proteins demonstrated that the predicted folding core also harbors residues that form native-like interactions early in the folding reaction. In the current work, we have tested our empirical potential functions on structurally-different proteins for which the folding cores have been revealed by protein hydrogen-deuterium exchange experiments. Using a set of 29 unrelated proteins, which have been extensively studied in the literature, we demonstrate that the average prediction result from our method is significantly better than predictions based on other computational methods. Our study is an important step towards the ultimate goal of understanding the correlation between folding cores and native structures.
authors.affiliation: Graduate Program of Structural and Computational Biology and Molecular Biophysics, USA.
authors.forename: Mingzhi
authors.initials: M
authors.lastname: Chen
authors.forename: Athanasios D
authors.initials: AD
authors.lastname: Dousis
authors.forename: Yinghao
authors.initials: Y
authors.lastname: Wu
authors.forename: Pernilla
authors.initials: P
authors.lastname: Wittung-Stafshede
authors.forename: Jianpeng
authors.initials: J
authors.lastname: Ma
mesh_terms: D000818:Animals; D030562:Databases, Protein; D003903:Deuterium; D006801:Humans; D006859:Hydrogen; D008958:Models, Molecular; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins; D006859:Hydrogen; D003903:Deuterium