Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5376178 | Chemical Physics | 2008 | 8 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Giorgio Schirò, Michele Sclafani, Chiara Caronna, Francesca Natali, Marie Plazanet, Antonio Cupane,