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Article

A Natively Monomeric Deubiquitinase UCH-L1 Forms Highly Dynamic but Defined Metastable Oligomeric Folding Intermediates.

The journal of physical chemistry letters - 3 May 2018

Lee Yun-Tzai Cloud, Hsu Shang-Te Danny

Abstract excerpt

Oligomerization of misfolded protein species is implicated in many human disorders. Here we showed by size-exclusion chromatography-coupled multiangle light scattering (SEC-MALS) and small-angle X-ray scattering (SEC-SAXS) that urea-induced folding intermediate of human ubiquitin C-terminal hydrolase, UCH-L1, can form well-defined dimers and tetramers under denaturing conditions despite being highly disordered....

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PMID: 29688017
DOI: 10.1021/acs.jpclett.8b00815

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