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| Home > Publications database > Conformational dynamics of a protein in the folded and unfolded state |
| Journal Article | PreJuSER-30449 |
2003
Elsevier Science
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/S0301-0104(03)00144-7
Abstract: 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.
Keyword(s): J ; alpha-amylase (auto) ; quasielastic incoherent neutron scattering (auto) ; protein dynamics (auto) ; proteins in solution (auto) ; protein stability (auto)
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