Structural fluctuations and aging processes in deeply frozen proteins

Frozen proteins are nonergodic systems and are subject to two types of structural motions, namely relaxation and fluctuation. Relaxation manifests itself in aging processes which slow the fluctuations. Within certain approximations we are able to experimentally separate the aging dynamics from the f...

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Published in:Физика низких температур
Date:2003
Main Authors: Schlichter, J., Ponkratov, V.V., Friedrich, J.
Format: Article
Language:English
Published: Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України 2003
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Online Access:https://nasplib.isofts.kiev.ua/handle/123456789/128929
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Journal Title:Digital Library of Periodicals of National Academy of Sciences of Ukraine
Cite this:Structural fluctuations and aging processes in deeply frozen proteins / J. Schlichter, V.V. Ponkratov, J. Friedrich // Физика низких температур. — 2003. — Т. 29, № 9-10. — С. 1049-1056. — Бібліогр.: 21 назв. — англ.

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Digital Library of Periodicals of National Academy of Sciences of Ukraine
id nasplib_isofts_kiev_ua-123456789-128929
record_format dspace
spelling Schlichter, J.
Ponkratov, V.V.
Friedrich, J.
2018-01-14T13:04:47Z
2018-01-14T13:04:47Z
2003
Structural fluctuations and aging processes in deeply frozen proteins / J. Schlichter, V.V. Ponkratov, J. Friedrich // Физика низких температур. — 2003. — Т. 29, № 9-10. — С. 1049-1056. — Бібліогр.: 21 назв. — англ.
0132-6414
PACS: 87.15.-v
https://nasplib.isofts.kiev.ua/handle/123456789/128929
Frozen proteins are nonergodic systems and are subject to two types of structural motions, namely relaxation and fluctuation. Relaxation manifests itself in aging processes which slow the fluctuations. Within certain approximations we are able to experimentally separate the aging dynamics from the fluctuation dynamics by introducing two time parameters, namely an aging time ta and a waiting time tw. Both processes follow power laws in time. The fluctuation dynamics shows features of universality characterized by a rather uniform exponent of 1/4. This universality features were shown to be possible due to a random walk on a 1D random trajectory in conformational phase space. A very interesting aspect of protein dynamics concerns the influence of the host solvent on structural motions of the protein cores. We present results for sugar solvents and discuss possible mechanisms.
Support from the DFG (SFB 533, B5) and from the Fonds der Chemischen Industrie is gratefully acknowledged.
en
Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України
Физика низких температур
Biological Systems at Low Temperatures
Structural fluctuations and aging processes in deeply frozen proteins
Article
published earlier
institution Digital Library of Periodicals of National Academy of Sciences of Ukraine
collection DSpace DC
title Structural fluctuations and aging processes in deeply frozen proteins
spellingShingle Structural fluctuations and aging processes in deeply frozen proteins
Schlichter, J.
Ponkratov, V.V.
Friedrich, J.
Biological Systems at Low Temperatures
title_short Structural fluctuations and aging processes in deeply frozen proteins
title_full Structural fluctuations and aging processes in deeply frozen proteins
title_fullStr Structural fluctuations and aging processes in deeply frozen proteins
title_full_unstemmed Structural fluctuations and aging processes in deeply frozen proteins
title_sort structural fluctuations and aging processes in deeply frozen proteins
author Schlichter, J.
Ponkratov, V.V.
Friedrich, J.
author_facet Schlichter, J.
Ponkratov, V.V.
Friedrich, J.
topic Biological Systems at Low Temperatures
topic_facet Biological Systems at Low Temperatures
publishDate 2003
language English
container_title Физика низких температур
publisher Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України
format Article
description Frozen proteins are nonergodic systems and are subject to two types of structural motions, namely relaxation and fluctuation. Relaxation manifests itself in aging processes which slow the fluctuations. Within certain approximations we are able to experimentally separate the aging dynamics from the fluctuation dynamics by introducing two time parameters, namely an aging time ta and a waiting time tw. Both processes follow power laws in time. The fluctuation dynamics shows features of universality characterized by a rather uniform exponent of 1/4. This universality features were shown to be possible due to a random walk on a 1D random trajectory in conformational phase space. A very interesting aspect of protein dynamics concerns the influence of the host solvent on structural motions of the protein cores. We present results for sugar solvents and discuss possible mechanisms.
issn 0132-6414
url https://nasplib.isofts.kiev.ua/handle/123456789/128929
citation_txt Structural fluctuations and aging processes in deeply frozen proteins / J. Schlichter, V.V. Ponkratov, J. Friedrich // Физика низких температур. — 2003. — Т. 29, № 9-10. — С. 1049-1056. — Бібліогр.: 21 назв. — англ.
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first_indexed 2025-12-07T16:40:17Z
last_indexed 2025-12-07T16:40:17Z
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