Protein dynamics

Fritz Parak; Hans Frauenfelder

doi:10.1016/0378-4371(93)90431-3

Protein dynamics

Fritz Parak
, Hans Frauenfelder

Johannes Gutenberg University
Los Alamos National Laboratory
University of Illinois

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

Abstract

Protein dynamics reveals the complexity of these biomolecules. The structural fluctuations and relaxations are determined by a rugged energy landscape where the vallies, the conformational substates, are arranged in a hierarchy of tiers. Several experimental techniques have been used to study the different aspects of protein dynamics. We discuss X-ray structure determinations and pressure tuned hole burning experiments to study structural distributions. Equilibrium fluctuations have been studied by Mössbauer spectroscopy, Rayleigh scattering of Mössbauer radiation and incoherent neutron scattering. Most results on structural relaxations have been obtained from the CO rebinding kinetics in CO ligated myoglobin after flash-photolysis. In addition some Mössbauer investigations of structural relaxation are discussed.

Original language	English
Pages (from-to)	332-345
Number of pages	14
Journal	Physica A: Statistical Mechanics and its Applications
Volume	201
Issue number	1-3
DOIs	https://doi.org/10.1016/0378-4371(93)90431-3
State	Published - 1 Dec 1993
Externally published	Yes

Access to Document

10.1016/0378-4371(93)90431-3

Cite this

@article{c99a0099008547999dda32e5f40a2289,

title = "Protein dynamics",

abstract = "Protein dynamics reveals the complexity of these biomolecules. The structural fluctuations and relaxations are determined by a rugged energy landscape where the vallies, the conformational substates, are arranged in a hierarchy of tiers. Several experimental techniques have been used to study the different aspects of protein dynamics. We discuss X-ray structure determinations and pressure tuned hole burning experiments to study structural distributions. Equilibrium fluctuations have been studied by M{\"o}ssbauer spectroscopy, Rayleigh scattering of M{\"o}ssbauer radiation and incoherent neutron scattering. Most results on structural relaxations have been obtained from the CO rebinding kinetics in CO ligated myoglobin after flash-photolysis. In addition some M{\"o}ssbauer investigations of structural relaxation are discussed.",

author = "Fritz Parak and Hans Frauenfelder",

note = "Funding Information: Support from the Deutsche Forschungsgemeinschafatn d the Fonds der Chemie is gratefully acknowledged.",

year = "1993",

month = dec,

day = "1",

doi = "10.1016/0378-4371(93)90431-3",

language = "English",

volume = "201",

pages = "332--345",

journal = "Physica A: Statistical Mechanics and its Applications",

issn = "0378-4371",

publisher = "Elsevier B.V.",

number = "1-3",

}

TY - JOUR

T1 - Protein dynamics

AU - Parak, Fritz

AU - Frauenfelder, Hans

N1 - Funding Information: Support from the Deutsche Forschungsgemeinschafatn d the Fonds der Chemie is gratefully acknowledged.

PY - 1993/12/1

Y1 - 1993/12/1

N2 - Protein dynamics reveals the complexity of these biomolecules. The structural fluctuations and relaxations are determined by a rugged energy landscape where the vallies, the conformational substates, are arranged in a hierarchy of tiers. Several experimental techniques have been used to study the different aspects of protein dynamics. We discuss X-ray structure determinations and pressure tuned hole burning experiments to study structural distributions. Equilibrium fluctuations have been studied by Mössbauer spectroscopy, Rayleigh scattering of Mössbauer radiation and incoherent neutron scattering. Most results on structural relaxations have been obtained from the CO rebinding kinetics in CO ligated myoglobin after flash-photolysis. In addition some Mössbauer investigations of structural relaxation are discussed.

AB - Protein dynamics reveals the complexity of these biomolecules. The structural fluctuations and relaxations are determined by a rugged energy landscape where the vallies, the conformational substates, are arranged in a hierarchy of tiers. Several experimental techniques have been used to study the different aspects of protein dynamics. We discuss X-ray structure determinations and pressure tuned hole burning experiments to study structural distributions. Equilibrium fluctuations have been studied by Mössbauer spectroscopy, Rayleigh scattering of Mössbauer radiation and incoherent neutron scattering. Most results on structural relaxations have been obtained from the CO rebinding kinetics in CO ligated myoglobin after flash-photolysis. In addition some Mössbauer investigations of structural relaxation are discussed.

UR - https://www.scopus.com/pages/publications/43949171955

U2 - 10.1016/0378-4371(93)90431-3

DO - 10.1016/0378-4371(93)90431-3

M3 - Article

AN - SCOPUS:43949171955

SN - 0378-4371

VL - 201

SP - 332

EP - 345

JO - Physica A: Statistical Mechanics and its Applications

JF - Physica A: Statistical Mechanics and its Applications

IS - 1-3

ER -

Protein dynamics

Abstract

Access to Document

Other files and links

Fingerprint

Cite this