ReviewPhotosynthesis research
Protein dynamics investigated by neutron scattering.
Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Recent Progress in Solution Structure Studies of Photosynthetic Proteins Using Small-Angle Scattering Methods.Molecules (Basel, Switzerland) · 2023Review
- Comparison of tryptophan fluorescence lifetimes in cyanobacterial photosystem I frozen in the light and in the dark.Photosynthesis research · 2019Article
- Rate-limiting steps in the dark-to-light transition of Photosystem II - revealed by chlorophyll-a fluorescence induction.Scientific reports · 2018Article
- Solution structure of monomeric and trimeric photosystem I of Thermosynechococcus elongatus investigated by small-angle X-ray scattering.Photosynthesis research · 2017Article
- Gernot Renger (1937-2013): his life, Max-Volmer Laboratory, and photosynthesis research.Photosynthesis research · 2016Article
- Weak temperature dependence of P (+) H A (-) recombination in mutant Rhodobacter sphaeroides reaction centers.Photosynthesis research · 2016Article
- Structure/function/dynamics of photosystem II plastoquinone binding sites.Current protein & peptide science · 2014Review
- Perspectives in biological physics: the nDDB project for a neutron Dynamics Data Bank for biological macromolecules.The European physical journal. E, Soft matter · 2013Article
- Dynamic properties of photosystem II membranes at physiological temperatures characterized by elastic incoherent neutron scattering. Increased flexibility associated with the inactivation of the oxygen evolving complex.Photosynthesis research · 2012Article
- SANS investigation of the photosynthetic machinery of Chloroflexus aurantiacus.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 Q(A)(-·) reoxidation by Q(B) 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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.