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000030449 084__ $$2WoS$$aChemistry, Physical
000030449 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical
000030449 1001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b0$$uFZJ
000030449 245__ $$aConformational dynamics of a protein in the folded and unfolded state
000030449 260__ $$aAmsterdam [u.a.]$$bElsevier Science$$c2003
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000030449 440_0 $$09841$$aChemical Physics$$v292$$x0301-0104
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000030449 520__ $$aIn a quasielastic neutron scattering experiment, the picosecond dynamics of alpha-amylase was investigated for the folded and the unfolded state of the protein. In order to ensure a reasonable interpretation of the internal protein dynamics, the protein was measured in D2O-buffer solution. The much higher structural flexibility of the pH induced unfolded state as compared to the native folded state was quantified using a simple analytical model, describing a local diffusion inside a sphere. In terms of this model the conformational volume, which is explored mainly by confined protein side-chain movements, is parameterized by the radius of a sphere (folded state, r = 1.2 Angstrom; unfolded state, 1.8 Angstrom). Differences in conformational dynamics between the folded and the unfolded state of a protein are of fundamental interest in the field of protein science, because they are assumed to play an important role for the thermodynamics of folding/unfolding transition and for protein stability. (C) 2003 Elsevier Science B.V. All rights reserved.
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000030449 65320 $$2Author$$aalpha-amylase
000030449 65320 $$2Author$$aquasielastic incoherent neutron scattering
000030449 65320 $$2Author$$aprotein dynamics
000030449 65320 $$2Author$$aproteins in solution
000030449 65320 $$2Author$$aprotein stability
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