Picosecond conformational transition and equilibration of a cyclic peptide

AUTOR(ES)

Bredenbeck, Jens

FONTE

National Academy of Sciences

RESUMO

Ultrafast IR spectroscopy is used to monitor the nonequilibrium backbone dynamics of a cyclic peptide in the amide I vibrational range with picosecond time resolution. A conformational change is induced by means of a photoswitch integrated into the peptide backbone. Although the main conformational change of the backbone is completed after only 20 ps, the subsequent equilibration in the new region of conformational space continues for times >16 ns. Relaxation and equilibration processes of the peptide backbone occur on a discrete hierarchy of time scales. Albeit possessing only a few conformational degrees of freedom compared with a protein, the peptide behaves highly nontrivially and provides insights into the complexity of fast protein folding.

Documentos Relacionados

• Conformational transition of amyloid β-peptide
• Direct observation of sub-picosecond equilibration of excitation energy in the light-harvesting antenna of Rhodospirillum rubrum.
• Conformational Energy Studies of Oxytocin and Its Cyclic Moiety
• Conformational transition in DNA on a cold surface
• Global mapping of nucleic acid conformational space: dinucleoside monophosphate conformations and transition pathways among conformational classes