title: Effect of salt on the formation of salt-bridges in β-hairpin peptides.
abstract: Salt-bridges ubiquitously form between oppositely charged moieties in proteins. Here we quantify changes in population of salt-bridged β-hairpin peptides due to added salt, and determine the thermodynamic driving forces and cooperativity of salt-bridge formation under these conditions. We find only a fraction of salt-bridged folded conformations at physiologically relevant salt concentrations.
authors.affiliation: Institute of Chemistry and The Fritz Haber Research Center, Hebrew University of Jerusalem, Jerusalem, 91904, Israel. daniel@fh.huji.ac.il.
authors.forename: Shahar
authors.initials: S
authors.lastname: Sukenik
authors.forename: Yoav
authors.initials: Y
authors.lastname: Boyarski
authors.forename: Daniel
authors.initials: D
authors.lastname: Harries
mesh_terms: D006860:Hydrogen Bonding; D008956:Models, Chemical; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D012492:Salts / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D010446:Peptide Fragments; D012492:Salts