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

被引：21

作者：

Bizzarri, AR

Paciaroni, A

Arcangeli, C

Cannistraro, S ^{[1
]}

机构：

[1] Univ Tuscia, Dipartimento Sci Ambientali, INFM, I-01100 Viterbo, Italy

[2] Inst Max Von Laue Paul Langevin, INFM, Operat Grp Grenoble, F-38042 Grenoble, France

来源：

EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2001年 / 30卷 / 06期

关键词：

protein dynamics; boson peak; plastocyanin;

D O I：

10.1007/s002490100167

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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 nonexchangeable 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 I meV. These vibrational peaks are discussed in connection with the topological disorder of the systems and the fluctuations of the intramolecular hydrogen bonds.

引用

页码：443 / 449

页数：7

共 31 条

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