title: Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking.
abstract: Disulfide bonds between Cys residues in adjacent strands of parallel β-sheets are rare among proteins, which suggests that parallel β-sheet structure is not stabilized by such disulfide cross-links. We report experimental results that show, surprisingly, that an interstrand disulfide bond can stabilize parallel β-sheets formed by an autonomously folding peptide in aqueous solution. NMR analysis reveals that parallel β-sheet structure is terminated beyond the disulfide bond, which causes deviation from the extended backbone conformation at one of the Cys residues.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706, USA.
authors.forename: Aaron M
authors.initials: AM
authors.lastname: Almeida
authors.forename: Rebecca
authors.initials: R
authors.lastname: Li
authors.forename: Samuel H
authors.initials: SH
authors.lastname: Gellman
mesh_terms: D004220:Disulfides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D004220:Disulfides; D010455:Peptides