Dynamics of an antibiotic oligopeptide

Neutron time-of-flight spectra were measured for an H 2O-hydrated and a nominally dry sample of a 15-residue antibacterial oligopeptide from 99 to 271 K. Proton mobilities, quasielastic broadenings, and changes in low-frequency inelastic intensities characterise the evolution of the peptide energy l...

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Bibliographic Details
Published in:Physica. B, Condensed matter Condensed matter, 2006-11, Vol.385, p.874-876
Main Authors: Middendorf, H.D., Alves, N., Zanotti, J.-M., Gomes, P., Bastos, M.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Boson peak
Fundamental and applied biological sciences. Psychology
General aspects
Inelastic scattering
Molecular biophysics
Peptide dynamics
Proton mobilities
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Summary:Neutron time-of-flight spectra were measured for an H 2O-hydrated and a nominally dry sample of a 15-residue antibacterial oligopeptide from 99 to 271 K. Proton mobilities, quasielastic broadenings, and changes in low-frequency inelastic intensities characterise the evolution of the peptide energy landscape as a function of momentum transfer and temperature.
ISSN:0921-4526
1873-2135
DOI:10.1016/j.physb.2006.05.131