Fluctuations of conformational states in biological molecules

Theory for anomalous spectral diffusion dynamics

A. L. Burin, Yu A. Berlin, A. Z. Patashinski, Mark A Ratner, J. Friedrich

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

An anomalous power law behavior of spectral diffusion broadening of persistent holes is found in large biological molecules dissolved in a glassy host at very low temperature. We argue that this is caused by the internal degrees of freedom of the biomolecule itself rather than by excitations of the glassy host. To explain the observed universal time dependence of the hole width w ∼ t1/4, we propose a stochastic model of protein dynamics close to the equilibrium, which describes this process in terms of the quasi-one-dimensional diffusion of proteins in conformation space. Assuming that each step of diffusive motion changes the electronic excitation energy randomly, we derive the observed time behavior of the spectral hole. The physical mechanisms involved are discussed.

Original languageEnglish
Pages (from-to)321-323
Number of pages3
JournalPhysica B: Condensed Matter
Volume316-317
DOIs
Publication statusPublished - May 2002

Fingerprint

Proteins
Molecules
Excitation energy
Biomolecules
Stochastic models
universal time
proteins
Conformations
molecules
excitation
time dependence
degrees of freedom
electronics
Temperature
energy

Keywords

  • Hole burning
  • Proteins
  • Spectral diffusion
  • Strain interaction

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics

Cite this

Fluctuations of conformational states in biological molecules : Theory for anomalous spectral diffusion dynamics. / Burin, A. L.; Berlin, Yu A.; Patashinski, A. Z.; Ratner, Mark A; Friedrich, J.

In: Physica B: Condensed Matter, Vol. 316-317, 05.2002, p. 321-323.

Research output: Contribution to journalArticle

Burin, A. L. ; Berlin, Yu A. ; Patashinski, A. Z. ; Ratner, Mark A ; Friedrich, J. / Fluctuations of conformational states in biological molecules : Theory for anomalous spectral diffusion dynamics. In: Physica B: Condensed Matter. 2002 ; Vol. 316-317. pp. 321-323.
@article{237c1e4b9a11455b9dde7cfceb64c111,
title = "Fluctuations of conformational states in biological molecules: Theory for anomalous spectral diffusion dynamics",
abstract = "An anomalous power law behavior of spectral diffusion broadening of persistent holes is found in large biological molecules dissolved in a glassy host at very low temperature. We argue that this is caused by the internal degrees of freedom of the biomolecule itself rather than by excitations of the glassy host. To explain the observed universal time dependence of the hole width w ∼ t1/4, we propose a stochastic model of protein dynamics close to the equilibrium, which describes this process in terms of the quasi-one-dimensional diffusion of proteins in conformation space. Assuming that each step of diffusive motion changes the electronic excitation energy randomly, we derive the observed time behavior of the spectral hole. The physical mechanisms involved are discussed.",
keywords = "Hole burning, Proteins, Spectral diffusion, Strain interaction",
author = "Burin, {A. L.} and Berlin, {Yu A.} and Patashinski, {A. Z.} and Ratner, {Mark A} and J. Friedrich",
year = "2002",
month = "5",
doi = "10.1016/S0921-4526(02)00497-0",
language = "English",
volume = "316-317",
pages = "321--323",
journal = "Physica B: Condensed Matter",
issn = "0921-4526",
publisher = "Elsevier",

}

TY - JOUR

T1 - Fluctuations of conformational states in biological molecules

T2 - Theory for anomalous spectral diffusion dynamics

AU - Burin, A. L.

AU - Berlin, Yu A.

AU - Patashinski, A. Z.

AU - Ratner, Mark A

AU - Friedrich, J.

PY - 2002/5

Y1 - 2002/5

N2 - An anomalous power law behavior of spectral diffusion broadening of persistent holes is found in large biological molecules dissolved in a glassy host at very low temperature. We argue that this is caused by the internal degrees of freedom of the biomolecule itself rather than by excitations of the glassy host. To explain the observed universal time dependence of the hole width w ∼ t1/4, we propose a stochastic model of protein dynamics close to the equilibrium, which describes this process in terms of the quasi-one-dimensional diffusion of proteins in conformation space. Assuming that each step of diffusive motion changes the electronic excitation energy randomly, we derive the observed time behavior of the spectral hole. The physical mechanisms involved are discussed.

AB - An anomalous power law behavior of spectral diffusion broadening of persistent holes is found in large biological molecules dissolved in a glassy host at very low temperature. We argue that this is caused by the internal degrees of freedom of the biomolecule itself rather than by excitations of the glassy host. To explain the observed universal time dependence of the hole width w ∼ t1/4, we propose a stochastic model of protein dynamics close to the equilibrium, which describes this process in terms of the quasi-one-dimensional diffusion of proteins in conformation space. Assuming that each step of diffusive motion changes the electronic excitation energy randomly, we derive the observed time behavior of the spectral hole. The physical mechanisms involved are discussed.

KW - Hole burning

KW - Proteins

KW - Spectral diffusion

KW - Strain interaction

UR - http://www.scopus.com/inward/record.url?scp=0036567161&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036567161&partnerID=8YFLogxK

U2 - 10.1016/S0921-4526(02)00497-0

DO - 10.1016/S0921-4526(02)00497-0

M3 - Article

VL - 316-317

SP - 321

EP - 323

JO - Physica B: Condensed Matter

JF - Physica B: Condensed Matter

SN - 0921-4526

ER -