English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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

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