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Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy

G. Chen ; P. W. Fenimore ; H. Frauenfelder ; F. Mezei ; Jan Swenson (Institutionen för teknisk fysik, Kondenserade materiens fysik) ; R. D. Young
PHILOSOPHICAL MAGAZINE (1478-6435). Vol. 88 (2008), 33-35, p. 3877-3883.
[Konferensbidrag, refereegranskat]

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.

Nyckelord: protein dynamics, hydration shell, beta fluctuations, inelastic neutron, scattering, dielectric relaxation spectroscopy, no dynamical transitions



Denna post skapades 2009-10-26. Senast ändrad 2016-07-21.
CPL Pubid: 100767

 

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Institutioner (Chalmers)

Institutionen för teknisk fysik, Kondenserade materiens fysik (1900-2015)

Ämnesområden

Teknisk fysik

Chalmers infrastruktur