%0 Journal Article
%A Fitter, J.
%T Conformational dynamics of a protein in the folded and unfolded state
%J Chemical physics
%V 292
%@ 0301-0104
%C Amsterdam [u.a.]
%I Elsevier Science
%M PreJuSER-30449
%P 405 - 411
%D 2003
%Z Record converted from VDB: 12.11.2012
%X In a quasielastic neutron scattering experiment, the picosecond dynamics of alpha-amylase was investigated for the folded and the unfolded state of the protein. In order to ensure a reasonable interpretation of the internal protein dynamics, the protein was measured in D2O-buffer solution. The much higher structural flexibility of the pH induced unfolded state as compared to the native folded state was quantified using a simple analytical model, describing a local diffusion inside a sphere. In terms of this model the conformational volume, which is explored mainly by confined protein side-chain movements, is parameterized by the radius of a sphere (folded state, r = 1.2 Angstrom; unfolded state, 1.8 Angstrom). Differences in conformational dynamics between the folded and the unfolded state of a protein are of fundamental interest in the field of protein science, because they are assumed to play an important role for the thermodynamics of folding/unfolding transition and for protein stability. (C) 2003 Elsevier Science B.V. All rights reserved.
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000184511200032
%R 10.1016/S0301-0104(03)00144-7
%U https://juser.fz-juelich.de/record/30449