title: Computer determination of peptide conformations in water: different roads to structure.
abstract: Fragments of proteins (short peptides) that "fold" suggest a mechanism of how complete conformational search in protein folding is avoided. We used a computational method to determine structures of two foldable peptides in explicit water: RVEW and CSVTC. The optimization starts from random structures and no experimental constraints are used. In agreement with NMR data, the simulations find a hydrophobic pair (Val/Trp) in REVW. The structure of CSVTC is induced by a surface water that bridges two amide hydrogens, a drive to structure hypothesized by Ben-Naim [Ben-Naim, A. (1990) J. Chem. Phys. 93, 8196-8210] that is largely ignored in studies of folding. Tendency to structure in short peptide chains suggests a mechanism for the formation of short-range nucleation sites in protein folding.
authors.affiliation: Department of Chemistry, University of Illinois, Chicago 60607-7061, USA.
authors.forename: C L
authors.initials: CL
authors.lastname: Simmerling
authors.forename: R
authors.initials: R
authors.lastname: Elber
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012996:Solutions; D014867:Water / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D012996:Solutions; D014867:Water