M -C Bellissent-Funel
Articles written in Pramana – Journal of Physics
Volume 63 Issue 1 July 2004 pp 91-97
It is well-known that water plays a major role in the stability and catalytic function of proteins. Both the effect of hydration water on the dynamics of proteins and that of proteins on the dynamics of water have been studied using inelastic neutron scattering. Inelastic neutron scattering is the most direct probe of diffusive protein dynamics on the picosecond-nanosecond time-scale. We present here results relative to a photosynthetic globular protein, the C-phycocyanin, that can be obtained in protonated and deuterated forms. Diffusive motions have been studied using the protonated C-phycocyanin, protein. Molecular dynamics simulation and analytical theory have been combined to analyse the data and get a detailed description of diffusive motions for protein. The simulation-derived dynamic structure factors are in good agreement with experiment. The dynamical parameters are shown to present a smooth variation with distance from the core of the protein. The collective dynamics has been investigated using the fully deuterated C-phycocyanin protein. Both the experimental and calculated spectra exhibit a dynamic relaxation with a characteristic time of about 10 ps.
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