TY  - JOUR
AU  - Monkenbusch, M.
AU  - Richter, D.
AU  - Biehl, R.
TI  - Observation of protein domain motions by neutron spectroscopy
JO  - ChemPhysChem
VL  - 11
SN  - 1439-4235
CY  - Weinheim
PB  - Wiley-VCH Verl.
M1  - PreJuSER-11981
SP  - 1187 - 1194
PY  - 2010
N1  - Record converted from VDB: 12.11.2012
AB  - High-resolution inelastic neutron scattering, which is available with neutron spin-echo spectroscopy (NSE) is introduced as a tool for the analysis of biomolecule flexibility. Coherent scattering in a range where it is sensitive to length scales of nanometers and covering a time range from picoseconds to several 100 ns makes the motion of larger subdomains within proteins visible. We show that and how the internal domain motion within a protein in solution can be measured. Comparison with displacement patterns from normal mode analysis provides further insight into the nature of the geometry of the motions that lead to the observed dynamic signature. The NSE experiment on alcohol dehydrogenase (ADH) is used as example to illustrate the general principles of the method.
KW  - Alcohol Dehydrogenase: chemistry
KW  - Molecular Dynamics Simulation
KW  - NAD: chemistry
KW  - Neutron Diffraction
KW  - Protein Structure, Tertiary
KW  - NAD (NLM Chemicals)
KW  - Alcohol Dehydrogenase (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19924753
UR  - <Go to ISI:>//WOS:000277666900010
DO  - DOI:10.1002/cphc.200900514
UR  - https://juser.fz-juelich.de/record/11981
ER  -