title: Side-chain and backbone ordering in a polypeptide.
abstract: We report results from multicanonical simulations of polyglutamic acid chains of length of ten residues. For this simple polypeptide we observe a decoupling of backbone and side-chain ordering in the folding process. While the details of the two transitions vary between the peptide in gas phase and in an implicit solvent, our results indicate that, independent of the specific surroundings, upon continuously lowering the temperature side-chain ordering occurs only after the backbone topology is completely formed.
authors.affiliation: Department of Physics, Michigan Technological University, Houghton, Michigan 49931, USA. yawei@mtu.edu
authors.forename: Yanjie
authors.initials: Y
authors.lastname: Wei
authors.forename: Walter
authors.initials: W
authors.lastname: Nadler
authors.forename: Ulrich H E
authors.initials: UH
authors.lastname: Hansmann
mesh_terms: D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013696:Temperature
chemical_list: D010455:Peptides