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Dielectric Relaxation in Biological SystemsPhysical Principles, Methods, and Applications$
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Valerica Raicu and Yuri Feldman

Print publication date: 2015

Print ISBN-13: 9780199686513

Published to Oxford Scholarship Online: August 2015

DOI: 10.1093/acprof:oso/9780199686513.001.0001

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Dielectric Spectroscopy of Hydrated Biomacromolecules

Dielectric Spectroscopy of Hydrated Biomacromolecules

(p.248) 3.3 Dielectric Spectroscopy of Hydrated Biomacromolecules
Dielectric Relaxation in Biological Systems

Masahiro Nakanishi

Alexei P. Sokolov

Oxford University Press

The chapter presents an overview of dielectric studies of hydrated protein dynamics. The dielectric data are compared to other experimental techniques (e.g. neutron scattering, simulations, and NMR). We emphasize the importance of explicit account for interfacial polarization effects in protein powders. Four dielectric processes are discussed. The main process, which has relaxation time ~10–50 ps at room temperature, is attributed to coupled protein–hydration water motions. The slow process, ~102–103 times slower than the main process, is ascribed to large-scale, domain-like motions of proteins. The anomalous intensity slow process (dielectric amplitude ~103–105) is 106–107 times slower than the main process and seems to be related to the glass transition of hydrated proteins. The process faster than the main process seems to be an artifact of earlier studies. The chapter suggests a general classification of the relaxation processes in hydrated proteins.

Keywords:   dielectric spectroscopy, neutron scattering spectroscopy, protein dynamics, hydration water, glass transition, dynamic transition, lysozyme, myoglobin, albumin

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