Multistep Protein Unfolding Scenarios from the Rupture of a Complex Metal Cluster Cd₃S₉.

ABSTRACT: Protein (un)folding is a complex and essential process. With the rapid development of single-molecule techniques, we can detect multiple and transient proteins (un)folding pathways/intermediates. However, the observation of multiple multistep (>2) unfolding scenarios for a single protein domain remains limited. Here, we chose metalloprotein with relatively stable and multiple metal-ligand coordination bonds as a system for such a purpose. Using AFM-based single-molecule force spectroscopy (SMFS), we successfully demonstrated the complex and multistep protein unfolding scenarios of the β-domain of a human protein metallothionein-3 (MT). MT is a protein of ~60 amino acids (aa) in length with 20 cysteines for various metal binding, and the β-domain (βMT) is of ~30 aa with an M₃S

SUBMITTER: Yuan G 

PROVIDER: S-EPMC6642161 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature