title: Folding thermodynamics of model four-strand antiparallel beta-sheet proteins.
abstract: The thermodynamic properties for three different types of off-lattice four-strand antiparallel beta-strand protein models interacting via a hybrid Go-type potential have been investigated. Discontinuous molecular dynamic simulations have been performed for different sizes of the bias gap g, an artificial measure of a model protein's preference for its native state. The thermodynamic transition temperatures are obtained by calculating the squared radius of gyration R(g)(2), the root-mean-squared pair separation fluctuation Delta(B), the specific heat C(v), the internal energy of the system E, and the Lindemann disorder parameter Delta(L). Despite these models' simplicity, they exhibit a complex set of protein transitions, consistent with those observed in experimental studies on real proteins. Starting from high temperature, these transitions include a collapse transition, a disordered-to-ordered globule transition, a folding transition, and a liquid-to-solid transition. The high temperature transitions, i.e., the collapse transition and the disordered-to-ordered globule transition, exist for all three beta-strand proteins, although the native-state geometry of the three model proteins is different. However the low temperature transitions, i.e., the folding transition and the liquid-to-solid transition, strongly depend on the native-state geometry of the model proteins and the size of the bias gap.
authors.affiliation: Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, USA. hbj@turbo.che.ncsu.edu
authors.forename: Hyunbum
authors.initials: H
authors.lastname: Jang
authors.forename: Carol K
authors.initials: CK
authors.lastname: Hall
authors.forename: Yaoqi
authors.initials: Y
authors.lastname: Zhou
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D015233:Models, Statistical; D008962:Models, Theoretical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature; D013816:Thermodynamics