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...

Повний опис

Збережено в:
Бібліографічні деталі
Дата:2003
Автори: Schlichter, J., Ponkratov, V.V., Friedrich, J.
Формат: Стаття
Мова:English
Опубліковано: Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України 2003
Назва видання:Физика низких температур
Теми:
Онлайн доступ:http://dspace.nbuv.gov.ua/handle/123456789/128929
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Назва журналу:Digital Library of Periodicals of National Academy of Sciences of Ukraine
Цитувати: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
Опис
Резюме: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.