Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy

被引：40

作者：

Chen, G. ^{[1
]}

Fenimore, P. W. ^{[1
]}

Frauenfelder, H. ^{[1
]}

Mezei, F. ^{[2
]}

Swenson, J. ^{[3
]}

Young, R. D. ^{[4
]}

机构：

[1] Los Alamos Natl Lab, Div Theoret, Los Alamos, NM 87545 USA

[2] Los Alamos Natl Lab, LANSCE, Los Alamos, NM USA

[3] Chalmers, Dept Appl Phys, S-41296 Gothenburg, Sweden

[4] No Arizona Univ, Dept Phys & Astron, Flagstaff, AZ 86011 USA

来源：

PHILOSOPHICAL MAGAZINE | 2008年 / 88卷 / 33-35期

关键词：

protein dynamics; hydration shell; beta fluctuations; inelastic neutron scattering; dielectric relaxation spectroscopy; no dynamical transitions;

D O I：

10.1080/14786430802585117

中图分类号：

T [工业技术];

学科分类号：

08 ;

摘要：

Glasses, supercooled liquids and proteins share common properties, in particular the existence of an energy landscape and the presence of two types of fluctuations, alpha and beta. While the effect of alpha fluctuations on proteins has been known for a few years, the effect of beta fluctuations has not been fully understood. By comparing neutron-scattering data on the protein myoglobin with beta fluctuations in the hydration shell measured by dielectric relaxation spectroscopy, we show that the internal protein motions are slaved to these fluctuations. We also show that there is no 'dynamical transition' in proteins near 200 K. The rapid increase in the mean-square displacement with temperature in many neutron-scattering experiments can be quantitatively predicted by beta fluctuations in the hydration shell.

引用

页码：3877 / 3883

页数：7

共 14 条

[1] Temperature dependence of fast fluctuations in single- and double-stranded DNA molecules: a neutron scattering investigation [J].

Cornicchi, E. ;

Capponi, S. ;

Marconi, M. ;

Onori, G. ;

Paciaroni, A. .

PHILOSOPHICAL MAGAZINE, 2007, 87 (3-5) :509-515

[2] Protein-water displacement distributions [J].

Doster, W ;

Settles, M .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2005, 1749 (02) :173-186

[3] DYNAMICAL TRANSITION OF MYOGLOBIN REVEALED BY INELASTIC NEUTRON-SCATTERING [J].

DOSTER, W ;

CUSACK, S ;

PETRY, W .

NATURE, 1989, 337 (6209) :754-756

[4] Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions [J].

Fenimore, PW ;

Frauenfelder, H ;

McMahon, BH ;

Young, RD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (40) :14408-14413

[5] Slaving: Solvent fluctuations dominate protein dynamics and functions [J].

Fenimore, PW ;

Frauenfelder, H ;

McMahon, BH ;

Parak, FG .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (25) :16047-16051

[6] THE ENERGY LANDSCAPES AND MOTIONS OF PROTEINS [J].

FRAUENFELDER, H ;

SLIGAR, SG ;

WOLYNES, PG .

SCIENCE, 1991, 254 (5038) :1598-1603

[7] Myoglobin: The hydrogen atom of biology and a paradigm of complexity [J].

Frauenfelder, H ;

McMahon, BH ;

Fenimore, PW .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (15) :8615-8617

[8] The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin [J].

Frauenfelder, H ;

McMahon, BH ;

Austin, RH ;

Chu, K ;

Groves, JT .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (05) :2370-2374

[9]

FRAUENFELDER H, 2008, P NATL SCI US UNPUB

[10] Protein dynamics studied by neutron scattering [J].

Gabel, F ;

Bicout, D ;

Lehnert, U ;

Tehei, M ;

Weik, M ;

Zaccai, G .

QUARTERLY REVIEWS OF BIOPHYSICS, 2002, 35 (04) :327-367

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