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  Librational fluctuations in protein glasses.

Marsh, D., Barlucci, R., Guzzi, R., Sportelli, L., & Esmann, M. (2013). Librational fluctuations in protein glasses. Biochimica et Biophysica Acta-Proteins and Proteomics, 1834(8), 1591-1595. doi:10.1016/j.bbapap.2013.05.001.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-3E9B-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CA52-F
Genre: Journal Article

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1833501.pdf (Publisher version), 342KB
 
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 Creators:
Marsh, D.1, Author              
Barlucci, R., Author
Guzzi, R., Author
Sportelli, L., Author
Esmann, M., Author
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1Emeritus Group of Spectroscopy and Photochemical Kinetics, MPI for Biophysical Chemistry, Max Planck Society, ou_578625              

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Free keywords: Glass transition; Arrhenius behaviour; Na,K-ATPase; Spin label; EPR
 Abstract: Librational motions in the region of the protein "glass" (or dynamic) transition are analysed for spin-labelled haemoglobin, serum albumin and beta-lactoglobulin by EPR spectroscopy. A discontinuity in the temperature dependence of the mean-square librational amplitude, <alpha(2)>, occurs in the region of 200 K as found for the mean-square atomic displacement, <r(2)>, at the protein dynamic transition by Mossbauer spectroscopy and neutron scattering. The discontinuity in <alpha(2)> vs. T can be described by the Vogel-Tammann-Fulcher equation, implying a finite glass transition temperature. Above the dynamic transition, <alpha(2)> vs. 1/T can be approximated by the Arrhenius law with activation energies similar to those usually found for <r(2)>, and relaxation processes in glass-forming media and the hydration shells of proteins. Similar results are found for librational fluctuations of membranous Na,K-ATPase spin-labelled either on superficial -SH groups or on those essential to activity.

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Language(s): eng - English
 Dates: 2013-05-102013-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bbapap.2013.05.001
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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
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Source Genre: Journal
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Pages: - Volume / Issue: 1834 (8) Sequence Number: - Start / End Page: 1591 - 1595 Identifier: ISSN: 1570-9639