Elisabetta Chiarparin

TL;DR: The use of LLS for competitive binding experiments to measure accurate dissociation constants of fragments that bind weakly to the ATP binding site of the N-terminal ATPase domain of heat shock protein 90 (Hsp90), a therapeutic target for cancer treatment is described.

TL;DR: A comprehensive description is presented of the effects on two-spin coherences of cross-correlation between the fluctuations of two different relaxation mechanisms in NMR (NMR) and rates show a high degree of correlation with the backbone Y angles in proteins.

TL;DR: In this article, it has been demonstrated that imperfections in RF-fields have little effect on efficiency of polarization transfer, provided that RF-amplitudes are comparable to magnitudes of heteronuclear scalar coupling constants, rendering this method ideal for selective experiments.

TL;DR: Structural-based drug design guided by structural information from X-ray crystallography, computational studies, and NMR solution conformational analysis was successfully applied to a fragment-derived lead resulting in AT-IAP, a potent, orally bioavailable, dual antagonist of XIAP and cIAP1 and a structurally novel chemical probe for IAP biology.

TL;DR: In this paper, it is demonstrated by expts and simulations that imperfections in RF fields have little effect on the efficiency of magnetization transfer, provided that the RF amplitudes are comparable with the magnitudes of the heteronuclear scalar coupling.