title: Simulation of coherent energy transfer in an alpha-helical peptide by Fermi resonance.
abstract: A mechanism by which NH stretching quanta are coherently transported along a chain of hydrogen bonded peptide groups is demonstrated by classical simulation of a section of the alpha-helical peptide poly(L-alanine). Vibrational motion takes place on a complex energy surface constructed from earlier ab initio and empirical surfaces. A speculative hypothesis of the biological role of this mechanism is presented, and the critical parameters governing the dynamics are identified and discussed.
authors.affiliation: Research School of Chemistry, Australian National University, Canberra, A.C.T.
authors.forename: D L
authors.initials: DL
authors.lastname: Clarke
authors.forename: M A
authors.initials: MA
authors.lastname: Collins
mesh_terms: D000081:Acetamides / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D055592:Biophysical Phenomena; D001703:Biophysics; D004735:Energy Transfer; D006860:Hydrogen Bonding; D008956:Models, Chemical; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D000081:Acetamides; D010455:Peptides; C019529:polyalanine; D000255:Adenosine Triphosphate; C018595:N-methylacetamide