Protein dynamics investigated by neutron scattering

This contribution describes incoherent quasielastic neutron scattering (QENS) as a suitable tool for investigations of protein dynamics with special emphasis on applications in photosynthesis research. QENS characterizes protein dynamics via the measurement of energy and momentum exchange between sa...

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Bibliographic Details
Published in:Photosynthesis research 2009-12, Vol.102 (2-3), p.281-293
Main Authors: Pieper, Jörg, Renger, Gernot
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Elasticity
Life Sciences
Neutron Diffraction - methods
Plant Genetics and Genomics
Plant Physiology
Plant Sciences
Proteins - chemistry
Review
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Summary:This contribution describes incoherent quasielastic neutron scattering (QENS) as a suitable tool for investigations of protein dynamics with special emphasis on applications in photosynthesis research. QENS characterizes protein dynamics via the measurement of energy and momentum exchange between sample system and incident low-energy neutrons (1 meV < E < 20 meV). This method is especially sensitive for picosecond motions of hydrogen atoms because it makes use of the exceptionally large incoherent neutron scattering cross section of protons and their almost homogeneous distribution in proteins. After a short introduction into the basic principles of neutron scattering, a more detailed description of QENS will be presented including a short overview on instrumentation and theory. Recent QENS results will be discussed for the antenna complex LHC II and PS II membrane fragments. It is shown that diffusive protein dynamics is indispensable for enabling [graphic removed] reoxidation by QB at temperatures above 240 K, which explains the strong dependence of this electron transfer step on temperature and hydration level of the sample. Finally, a new laser-QENS pump-probe technique will be introduced which permits in situ monitoring of protein dynamics correlated with a change of the functional state of the sample, i.e. a direct observation of structure-dynamics-function relationships in real time.
ISSN:0166-8595
1573-5079
DOI:10.1007/s11120-009-9480-9