title: 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
abstract: Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a single disulfide linkage. No evidence for any regular helical structure is found. Amide proton-solvent-exchange rate constants and 3JHN alpha coupling constants are evaluated.
authors.affiliation: Institute of Biological Physics, Pushchino, Russia.
authors.forename: M
authors.initials: M
authors.lastname: Okon
authors.forename: P
authors.initials: P
authors.lastname: Bray
authors.forename: D
authors.initials: D
authors.lastname: Vucelić
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009038:Motion; D011487:Protein Conformation; D012996:Solutions; D001613:beta 2-Microglobulin / Q000648:ultrastructure*
chemical_list: D012996:Solutions; D001613:beta 2-Microglobulin