TY  - JOUR
AU  - Fitter, J.
TI  - Conformational dynamics of a protein in the folded and unfolded state
JO  - Chemical physics
VL  - 292
SN  - 0301-0104
CY  - Amsterdam [u.a.]
PB  - Elsevier Science
M1  - PreJuSER-30449
SP  - 405 - 411
PY  - 2003
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000184511200032
DO  - DOI:10.1016/S0301-0104(03)00144-7
UR  - https://juser.fz-juelich.de/record/30449
ER  -