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Observation of Protein Domain Motions by Neutron Spectroscopy
Author(s) -
Monkenbusch Michael,
Richter Dieter,
Biehl Ralf
Publication year - 2010
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200900514
Subject(s) - neutron spin echo , neutron scattering , spectroscopy , picosecond , chemistry , neutron , biomolecule , scattering , neutron spectroscopy , inelastic neutron scattering , resolution (logic) , displacement (psychology) , physics , nuclear magnetic resonance , molecular physics , optics , nuclear physics , psychology , laser , quantum mechanics , artificial intelligence , computer science , psychotherapist , biochemistry
High‐resolution inelastic neutron scattering, which is available with neutron spin‐echo spectroscopy (NSE) is introduced as a tool for the analysis of biomolecule exibility. 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 oberved dynamic signature. The NSE experiment on alcohol dehydrogenase (ADH) is used as example to illustrate the general principles of the method.