ArticleJournal of the Royal Society, Interface2009
Coupled relaxations at the protein-water interface in the picosecond time scale.
Article in Journal of the Royal Society, Interface, 2009. 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.
- Hydration Contribution to the Solvation Free Energy of Water-Soluble Polymers.The journal of physical chemistry. B · 2025Article
- Molecular Dynamics Simulation of the Influence of Temperature and Salt on the Dynamic Hydration Layer in a Model Polyzwitterionic Polymer PAEDAPS.The journal of physical chemistry. B · 2023Article
- Why Proteins are Big: Length Scale Effects on Equilibria and Kinetics.The protein journal · 2019Review
- Evidence of a low-temperature dynamical transition in concentrated microgels.Science advances · 2018Article
- Dynamics of water bound to crystalline cellulose.Scientific reports · 2017Article
- The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.BMC biophysics · 2014Article
- Measurement of energy landscape roughness of folded and unfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.Biophysical journal · 2012Article
- From water and ions to crowded biomacromolecules: in vivo structuring of a prokaryotic cell.Microbiology and molecular biology reviews : MMBR · 2011Review
- Biological physics at large facilities: from molecule to cell.Journal of the Royal Society, Interface · 2009Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spectral behaviour of a protein and its hydration water has been investigated through neutron scattering. The availability of both hydrogenated and perdeuterated samples of maltose-binding protein (MBP) allowed us to directly measure with great accuracy the signal from the protein and the hydration water alone. Both the spectra of the MBP and its hydration water show two distinct relaxations, a behaviour that is reminiscent of glassy systems. The two components have been described using a phenomenological model that includes two Cole-Davidson functions. In MBP and its hydration water, the two relaxations take place with similar average characteristic times of approximately 10 and 0.2 ps. The common time scales of these relaxations suggest that they may be a preferential route to couple the dynamics of the water hydrogen-bond network around the protein surface with that of protein fluctuations.
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