ArticleBiophysical journal2008
Hydration dependence of active core fluctuations in bacteriorhodopsin.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- How can we derive hydration water dynamics with incoherent neutron scattering and molecular dynamics simulation?Biophysics and physicobiology · 2019Article
- Thermodynamics of lipid multi-lamellar vesicles in presence of sterols at high hydrostatic pressure.Scientific reports · 2017Article
- Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected byThe journal of physical chemistry. B · 2017Article
- The fluctuating ribosome: thermal molecular dynamics characterized by neutron scattering.Scientific reports · 2016Article
- The observation of evolutionary interaction pattern pairs in membrane proteins.BMC structural biology · 2015Article
- Zaccai neutron resilience and site-specific hydration dynamics in a globular protein.The European physical journal. E, Soft matter · 2013Article
- From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We used neutron scattering and specific hydrogen-deuterium labeling to investigate the thermal dynamics of isotope-labeled amino acids and retinal, predominantly in the active core and extracellular moiety of bacteriorhodopsin (BR) in the purple membrane and the dynamical response to hydration. Measurements on two neutron spectrometers allowed two populations of motions to be characterized. The lower amplitude motions were found to be the same for both the labeled amino acids and retinal of BR and the global membrane. The larger amplitude dynamics of the labeled part, however, were found to be more resilient than the average membrane, suggesting their functional importance. The response to hydration was characterized, showing that the labeled part of BR is not shielded from hydration effects. The results suggest that the inhibition of high-amplitude motions by lowering hydration may play a key role in the slowing down of the photocycle and the proton pumping activity of BR.
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Registered trials
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