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Chapter I2 - Neutron spectroscopy

from Part I - Molecular dynamics

Published online by Cambridge University Press:  05 November 2012

Igor N. Serdyuk
Affiliation:
Institute of Protein Research, Moscow
Nathan R. Zaccai
Affiliation:
University of Bristol
Joseph Zaccai
Affiliation:
Institut de Biologie Structurale, Grenoble
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Summary

Historical overview and introduction to biological applications

We recall from Chapter A1 that biological events occur on an immensely extended range of time scales – from the femtosecond of electronic rearrangements in the first step of vision, to the 109 years of evolution. Thermal energy is expressed as atomic fluctuations on the picosecond–nanosecond time scale that constitute the basis of molecular dynamics. These fluctuations are of particular interest in biophysics because they result from and reflect the forces that structure biological macromolecules and the atomic motions and molecular flexibility associated with biological activity.

Thermal energy propagates through solids in waves of atomic motion, such as the normal modes discussed in Chapters A3 and I1. We can estimate values for the frequencies, wavelengths and amplitudes of thermal excitation waves from an order of magnitude calculation, e.g. by considering the movement of a mass similar to the mass of an atom moving in a simple harmonic potential of energy equal to Boltzmann's constant multiplied by 300 K (ambient temperature). It turns out that the frequencies are of the order of 1012 s−1, while the wavelengths and amplitudes are on the ångström scale. We saw in Part E that the energy associated with thermal vibrations corresponds to the IR frequency range in optical spectroscopy. Similarly, neutron spectroscopy takes advantage of the fact that the energies of thermal neutron beams match vibrational energies in solids and liquids.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
, pp. 948 - 968
Publisher: Cambridge University Press
Print publication year: 2007

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References

Bée, M. (1988). Quasielastic Neutron Scattering. Bristol: Adam Hilger.Google Scholar
Smith, J. C. (1991). Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments. Q. Rev. Biophys., 24, 227–291.CrossRefGoogle ScholarPubMed
Gabel, F., Bicout, D., et al. (2002). Protein dynamics studied by neutron scattering. Q. Rev. Biophys., 35, 327–367.CrossRefGoogle ScholarPubMed
Tehei, M., Franzetti, B., et al. (2004). Adaptation to extreme environments: Macromolecular thermal dynamics in psychrophile, mesophile and thermophile bacteria compared, in-vivo, by neutron scattering. EMBO Rep., 5, 66–70.CrossRefGoogle Scholar

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