title: Structures of a peptide fragment of beta2-microglobulin studied by replica-exchange molecular dynamics simulations - towards the understanding of the mechanism of amyloid formation.
abstract: We investigate in detail the structural properties of the monomeric peptide fragment that corresponds to residues 21-31 of beta(2)-microglobulin. As a first step towards the understanding of the mechanism of the amyloid formation, we have performed a replica-exchange molecular dynamics simulation of this peptide with explicit water molecules. We analyze various structural properties as functions of temperature. Although the corresponding part of the native protein is a fully extended beta-strand, our results show that beta-hairpin structures are formed with high frequency around 310 K. We conjecture that this beta-hairpin formation is closely related to the amyloid fibrillogenesis.
authors.affiliation: Computational Materials Science Center, National Institute for Materials Science, Tsukuba, Ibaraki, Japan.
authors.forename: Masamichi
authors.initials: M
authors.lastname: Nishino
authors.forename: Yuji
authors.initials: Y
authors.lastname: Sugita
authors.forename: Takao
authors.initials: T
authors.lastname: Yoda
authors.forename: Yuko
authors.initials: Y
authors.lastname: Okamoto
mesh_terms: D000682:Amyloid / Q000096:biosynthesis*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D001613:beta 2-Microglobulin / Q000737:chemistry*
chemical_list: D000682:Amyloid; D010446:Peptide Fragments; D001613:beta 2-Microglobulin