title: The alpha-helix folds more rapidly at the C-terminus than at the N-terminus.
abstract: The helix-coil dynamics of different sections of an alpha-helical model peptide were observed separately by nanosecond temperature jump experiments with IR detection on a series of isotopically labeled peptides. The results show that the helix-coil dynamics of the alpha-helical C-terminus are faster than those of the N-terminus.
authors.affiliation: Department of Chemistry and Surface Science Research Centre, University of Liverpool, Liverpool L69 3BX, UK.
authors.forename: Angela
authors.initials: A
authors.lastname: Pozo Ramajo
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Petty
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Starzyk
authors.forename: Sean M
authors.initials: SM
authors.lastname: Decatur
authors.forename: Martin
authors.initials: M
authors.lastname: Volk
mesh_terms: D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature; D013997:Time Factors
chemical_list: D010455:Peptides