Stephen W. Fesik

TL;DR: An analysis of heteronuclear-NMR-based screening data is used to derive relationships between the ability of small molecules to bind to a protein and various parameters that describe the protein binding site and these allow for quantitative comparative analyses of protein binding sites for use in target assessment and validation, virtual ligand screening, and structure-based drug design.

TL;DR: K-Ras inhibition represents an attractive therapeutic strategy for many cancers, however, Ras activation and signaling is accomplished primarily through protein-protein interactions that typically lack well-defined binding pockets and have been difficult to target with small molecules.

TL;DR: There are subtle differences in the hydrophobic binding groove in Bcl-2 that may translate into differences in antiapoptotic activity for the two isoforms, according to NMR spectroscopy.

TL;DR: A pair of 16‐residue peptides were designed and synthesized that were predicted to have a high helix propensity while maintaining the interactions important for complexation with Bcl‐XL and exhibited an enhanced affinity for B cl‐XL.

TL;DR: The solution structure of the Fas death domain, as determined by NMR spectroscopy, is described and the region of the death domain involved in self-association and binding to the downstream signalling partner FADD is identified.