title: A theoretical study of beta-sheet models: is the formation of hydrogen-bond networks cooperative?
abstract: The cooperativity in terms of enthalpy contribution for beta-sheet formation of polyglycine models in a vacuum has been studied theoretically by using a repeating unit approach. No cooperativity is found in the parallel direction for both the parallel and antiparallel beta-sheets. Cooperativity in the perpendicular direction is dependent upon the residue number (m) in each beta-strand. While there is large cooperativity in the acetamide hydrogen-bond chain (m = 0), the cooperativity is not large in beta-sheet networks (m > 0). SCIPCM solvent model calculations also significantly reduce the cooperativity in hydrogen-bond chains. It is concluded that cooperativity is mainly due to long-range electrostatic interactions and not due to the resonance effect.
authors.affiliation: Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
authors.forename: Yi-Lei
authors.initials: YL
authors.lastname: Zhao
authors.forename: Yun-Dong
authors.initials: YD
authors.lastname: Wu
mesh_terms: D006860:Hydrogen Bonding; D008956:Models, Chemical; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins