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Publication Abstract from PubMed

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.

Redox- and metal-directed structural diversification in designed metalloprotein assemblies.,Kakkis A, Golub E, Choi TS, Tezcan FA Chem Commun (Camb). 2022 Jun 16;58(49):6958-6961. doi: 10.1039/d2cc02440c. PMID:35642584^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.