Redox- and metal-directed structural diversification in designed metalloprotein assemblies. Issue 49 (1st June 2022)

• Record Type: Journal Article
• Authors: Kakkis, Albert; Golub, Eyal; Choi, Tae Su; Tezcan, F. Akif
• Is Part Of: Chemical communications. Volume 58:Issue 49(2022)
• Page Start: 6958
• Page End: 6961
• Publication Date: 2022-06-01
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d2cc02440c
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. Abstract : Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown – through extensive structural and biophysical characterization – to access five distinct oligomeric states, exemplifying how the complex interplay between hydrophobic, metal–ligand, and reversible covalent interactions could be harnessed to obtain multiple, responsive protein architectures from a single building block.