title: beta-sheet hydrogen bonding patterns in cystine peptides.
abstract: Cystine peptides have been shown to adopt conformations in organic solvents that mimic small beta-sheets. Relative hydrogen bond strengths, beta-strand aggregation, and the identity of individual hydrogen bond donors and acceptors have been identified through hydrogen/deuterium exchange.
authors.affiliation: Department of Chemistry, Bowdoin College, Brunswick, Maine 04011, USA.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Cashman
authors.forename: Brian R
authors.initials: BR
authors.lastname: Linton
mesh_terms: D003553:Cystine / Q000737:chemistry*; D019281:Dimerization; D006860:Hydrogen Bonding; D007700:Kinetics; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides; D003553:Cystine