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• W2021711218 abstract "In order to clarify the role of hard confinement on protein dynamics, elastic and quasi-elastic neutron scattering experiments have been performed on ferric horse myoglobin in two different systems: the protein embedded in a porous silica matrix, and the corresponding hydrated protein powder. Elastic data have been analysed using two different models (dynamical heterogeneity and anharmonic double-well potential) that take into account deviations of elastic intensity from Gaussian behaviour. The profile of quasi-elastic spectra has been approximated by a combination of Lorentzian and Gaussian components. Comparison between the data relative to the two different samples indicates that geometrical confinement within the matrix plays a crucial role in protein dynamics and conformational stability, the effect of sol–gel encapsulation being essentially a reduction of large scale protein motions (α-relaxation) likely related to the slowing down of solvent confined diffusion." @default.
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• W2021711218 date "2008-04-01" @default.
• W2021711218 modified "2023-10-06" @default.
• W2021711218 title "Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study" @default.
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• W2021711218 doi "https://doi.org/10.1016/j.chemphys.2007.07.045" @default.
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