Distribution of conformational states as common source of g-and A-strain in the ESR spectra of proteins and glassesReport as inadecuate




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Abstract : Additional experimental evidence on the structural and dynamical similarity between proteins and glasses is provided by the analysis conducted on the ESR spectra, at different temperatures, of some copper proteins and of some Cu++-doped glasses formed by water and a second component NaOH, DMSO, alcohols. All the spectra taken at temperatures below ∼ 210 K display a significant g- and A-strain that consists in a progressive broadening and decrese in the intensity of the copper hyperfine lines as the order of mI increases I = 3-2 is the Cu nuclear spin. These spectral features are taken into account by using a theoretical model which attributes the random distribution of the electric ligand fields around the copper ions to a distribution of the conformational substate energies both in the proteins and in the amorphous materials.

Keywords : glass glass structure hyperfine field interactions condensed matter molecular biophysics paramagnetic resonance proteins





Author: Salvatore Cannistraro

Source: https://hal.archives-ouvertes.fr/



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