title: Folding of the GB1 hairpin peptide from discrete path sampling.
abstract: The discrete path sampling technique is used to calculate folding pathways of the 16-amino acid beta hairpin-forming sequence from residues 41-56 of the B1 domain of protein G. The folding time is obtained using master equation dynamics and kinetic Monte Carlo simulations, and the time evolution of different order parameters and occupation probabilities of groups of minima are calculated and used to characterize intermediates on the folding pathway.
authors.affiliation: University Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
authors.forename: David A
authors.initials: DA
authors.lastname: Evans
authors.forename: David J
authors.initials: DJ
authors.lastname: Wales
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary
chemical_list: C029152:G-substrate; D009419:Nerve Tissue Proteins; D010455:Peptides