title: Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G.
abstract: We have studied the unfolding and refolding pathway of a beta-hairpin fragment of protein G by using molecular dynamics. Although this fragment is small, it possesses several of the qualities ascribed to small proteins: cooperatively formed beta-sheet secondary structure and a hydrophobic "core" of packed side chains. At high temperatures, we find that the beta-hairpin unfolds through a series of sudden, discrete conformational changes. These changes occur between states that are identified with the folded state, a pair of partially unfolded kinetic intermediates, and the unfolded state. To study refolding at low temperatures, we perform a series of short simulations starting from the transition states of the discrete transitions determined by the unfolding simulations.
authors.affiliation: Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
authors.forename: V S
authors.initials: VS
authors.lastname: Pande
authors.forename: D S
authors.initials: DS
authors.lastname: Rokhsar
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: C029152:G-substrate; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011494:Protein Kinases