ArticleEuropean biophysics journal : EBJ2006
Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering.
Article in European biophysics journal : EBJ, 2006. 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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7 citing papers in PubMed, 24 citations in OpenAlex.
- An experimentally representative in-silico protocol for dynamical studies of lyophilised and weakly hydrated amorphous proteins.Communications chemistry · 2024Article
- Impact of Sucrose as Osmolyte on Molecular Dynamics of Mouse Acetylcholinesterase.Biomolecules · 2020Article
- From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.Biophysical journal · 2009Article
- Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering.European biophysics journal : EBJ · 2008Article
- The dynamical transition of proteins, concepts and misconceptions.European biophysics journal : EBJ · 2008Article
- Thermal fluctuations of DNA enclosed by glycerol-water glassy matrices: an elastic neutron scattering investigation.European biophysics journal : EBJ · 2008Article
- C-phycocyanin hydration water dynamics in the presence of trehalose: an incoherent elastic neutron scattering study at different energy resolutions.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynamics of lysozyme in the picosecond timescale has been studied when it is in dry and hydrated powder form and when it is embedded in glycerol, glycerol-water, glucose and glucose-water matrices. The investigation has been undertaken through elastic neutron scattering technique on the backscattering spectrometer IN13. The dynamics of dry powder and embedded-in-glucose lysozyme can be considered purely vibrational up to 100 K, where the onset of an anharmonic contribution takes place. This contribution can be attributed to the activation of methyl group reorientations and is described with an Arrhenius trend. An additional source of anharmonic dynamics appears at higher temperatures for lysozyme in hydrated powders and embedded in glycerol, glycerol-water and glucose-water matrices. This second process, also represented with an Arrhenius trend, corresponds to the so-called protein dynamical transition. Both the temperature where such a transition takes place and the magnitude of the protein mean square displacements depend on the environment. The dynamical response of the protein to temperature is put in relationship with its thermal stability.
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