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Low-frequency vibrational modes in proteins: A neutron scattering investigation

TitleLow-frequency vibrational modes in proteins: A neutron scattering investigation
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2001
AuthorsBizzarri, A.R., Paciaroni A., Arcangeli Caterina, and Cannistraro S.
JournalEuropean Biophysics Journal
Volume30
Pagination443-449
ISSN01757571
Keywordsarticle, Biophysics, Copper, deuterium, electron transport, Energy, Escherichia coli, Hydration, Hydrogen, hydrogen bond, Hydrogen Bonding, Isotopes, molecular dynamics, neutron scattering, Neutrons, plastocyanin, Protein, Protein Conformation, Protein Structure, Proteins, proton, proton transport, Radiation, Scattering, vibration
Abstract

The low-frequency dynamics of plastocyanin, an electron transfer copper protein, has been investigated by incoherent neutron scattering at different temperatures. The contribution to the dynamic structure factor arising from H/D exchangeable and non-exchangeable protein protons has been evaluated by analyzing two differently exchanged protein samples. The dynamic structure factor of a hydrated plastocyanin sample with all the exchangeable hydrogens (about 150) replaced by deuterium exhibits an excess of vibrational modes, at about 3.5 meV, reminiscent of the boson peak found in other proteins and glassy systems. When only fast exchangeable hydrogens (about 50) are substituted by deuterium, the protein, besides the above-mentioned peak, shows an additional peak at about 1 meV. These vibrational peaks are discussed in connection with the topological disorder of the systems and the fluctuations of the intramolecular hydrogen bonds.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0034773304&doi=10.1007%2fs002490100167&partnerID=40&md5=bae8afb72fd3515f7a7e634d76292429
DOI10.1007/s002490100167
Citation KeyBizzarri2001443