Librational fluctuations in protein glasses.

Marsh, D.; Barlucci, R.; Guzzi, R.; Sportelli, L.; Esmann, M.

doi:10.1016/j.bbapap.2013.05.001

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Librational fluctuations in protein glasses.

MPS-Authors

/persons/resource/persons15495

Marsh, D.
Emeritus Group of Spectroscopy and Photochemical Kinetics, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://www.sciencedirect.com/science?_ob=MiamiImageURL&_cid=272652&_user=38661&_pii=S1570963913001945&_check=y&_origin=article&_zone=toolbar&_coverDate=31-Aug-2013&view=c&originContentFamily=serial&wchp=dGLbVlS-zSkWb&md5=f7cdae8a499410eaf82bc14c1b679a82&pid=1-s2.0-S1570963913001945-main.pdf
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-3E9B-6

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.