Francesca Natali

TL;DR: The results provide direct experimental evidence that the first anharmonic activation of proteins is largely due to methyl group rotations entering the time window of the spectrometer used, and indicate that the dynamical transition occurring at approximately 230 K can be attributed, at least at the hydration level investigated, mainly to motions involving backbone fluctuations.

TL;DR: The results provide an enhanced view into the structure and function of the P2 protein from human myelin, which is able to bind both monomeric lipids inside its cavity and membrane surfaces.

TL;DR: Activation barriers and free energy values obtained for the protein dynamical transition allow us to make a connection with the two-well interaction potential of supercooled-confined water proposed to explain a low-density→high-density liquid-liquid transition.

TL;DR: A broad and significant effort towards instrumental and methodological development to facilitate biology experiments at neutron sources worldwide is reviewed.

TL;DR: It is shown that a rapid increase of hydrogen atoms fluctuations at about 220 K, analogous to the one observed in hydrated myoglobin powders, is also observed in a hydrated amino acids mixture with the chemical composition of myoglobin but lacking the polypeptide chain.