Conotoxins serve as useful model peptides to understand the effects of protein posttranslational modifications (PTMs). Here, we focus on proline hydroxylation and C-terminal amidation of conotoxins PIIIA and TIIIA. Structure and function assays highlight distinct roles of these PTMs in oxidative folding, structural integrity and activity at sodium channels, advancing our understanding of PTM function in conotoxin pharmacology. (Image credit: Anne C. Conibear.)

This article belongs to the collection: 70th Birthday tribute to Professor David Craik.

Native mass spectrometry (nMS) was applied to screen an electrophilic covalent fragment library to identify ligands for the surface exposed cysteine residues of a soluble protein (carbonic anhydrase III), to determine which cysteines were modified and to measure the simultaneous binding of an orthosteric noncovalent inhibitor and covalent fragment hit. (Image credit: S.-A. Poulsen and L. M. Sternicki.)

This article belongs to the collection: 70th Birthday tribute to Professor David Craik.

Mast cells of our immune system are generally difficult and expensive to maintain in vitro and, therefore, not economical to use in drug discovery. The development of a bioassay expressing the human mas-related G protein-coupled receptor-X2 receptor linked to potassium channels in a host cell offers a good alternative. (Image credit: Jan Tytgat.)

This article belongs to the collection: 70th Birthday tribute to Professor David Craik.