title: Surface-induced conformational changes in lattice model proteins by Monte Carlo simulation.
abstract: We present Monte Carlo simulations of thermal, structural, and dynamic properties of a 27-segment lattice model protein adsorbed to a solid surface. The protein consists of a sequence of A and B segments whose order and topological contact energy values are chosen so that a unique (3x3x3 cubic) folded state occurs in the absence of an adsorbing surface [E. I. Shakhnovich and M. Gutin, Proc. Natl. Acad. Sci. USA 90, 7195 (1993)]. The surface consists of a plane of sites that interact either (i) equally with all contacting protein segments (an equal affinity surface) or (ii) more strongly with type A contacting segments (an A affinity surface). For both surfaces, we find the conformational change of an initially folded protein to begin with a continuous transition to a structure where all segments contact the surface. This is followed by a partial refolding to a low energy state; this step is continuous and results in full surface contact for the equal affinity surface and is activated and results in significant loss of surface contact for the A affinity surface. We also observe a lesser (greater) degree of average surface contact in the equal (A) affinity surface with an increase in temperature.
authors.affiliation: Department of Chemical Engineering and Materials Science, Wayne State University, 5050 Anthony Wayne Drive, Detroit, Michigan 48202, USA.
authors.forename: Victoria
authors.initials: V
authors.lastname: Castells
authors.forename: Shaoxiong
authors.initials: S
authors.lastname: Yang
authors.forename: Paul R
authors.initials: PR
authors.lastname: Van Tassel
mesh_terms: D009010:Monte Carlo Method; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D011506:Proteins