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Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy
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- Chen, G. (author)
- Los Alamos National Laboratory
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- Fenimore, P. W. (author)
- Los Alamos National Laboratory
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- Frauenfelder, H. (author)
- Los Alamos National Laboratory
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- (creator_code:org_t)
- Informa UK Limited, 2008
- 2008
- English.
- In: Philosophical Magazine. - : Informa UK Limited. - 1478-6435 .- 1478-6443. ; 88:33-35, s. 3877-3883
- Conference paper (peer-reviewed)
Abstract
Subject headings
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- Glasses, supercooled liquids and proteins share common properties, in particular the existence of an energy landscape and the presence of two types of fluctuations, alpha and beta. While the effect of alpha fluctuations on proteins has been known for a few years, the effect of beta fluctuations has not been fully understood. By comparing neutron-scattering data on the protein myoglobin with beta fluctuations in the hydration shell measured by dielectric relaxation spectroscopy, we show that the internal protein motions are slaved to these fluctuations. We also show that there is no 'dynamical transition' in proteins near 200 K. The rapid increase in the mean-square displacement with temperature in many neutron-scattering experiments can be quantitatively predicted by beta fluctuations in the hydration shell.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Annan teknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Other Engineering and Technologies (hsv//eng)
Keyword
- dielectric relaxation spectroscopy
- protein dynamics
- beta fluctuations
- no dynamical transitions
- inelastic neutron
- scattering
- hydration shell
Publication and Content Type
- kon (subject category)
- ref (subject category)
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- Chalmers University of Technology
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