期刊
COMMUNICATIONS CHEMISTRY
卷 4, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s42004-021-00592-1
关键词
-
资金
- National Natural Science Foundation of China [11874309, 11474237]
- 111 project [B16029]
Research on Csp protein shows that it mainly folds and unfolds in a single step over a force range from 5 pN to 50 pN. The unfolding rates exhibit different force sensitivities below and above 8 pN, indicating a free energy landscape with two barriers and a transient intermediate state between them. These findings provide new insights into the protein folding mechanism of two-state proteins.
Cold shock protein (Csp) is a typical two-state folding model protein which has been widely studied by biochemistry and single molecule techniques. Recently two-state property of Csp was confirmed by atomic force microscopy (AFM) through direct pulling measurement, while several long-lifetime intermediate states were found by force-clamp AFM. We systematically studied force-dependent folding and unfolding dynamics of Csp using magnetic tweezers with intrinsic constant force capability. Here we report that Csp mostly folds and unfolds with a single step over force range from 5 pN to 50 pN, and the unfolding rates show different force sensitivities at forces below and above similar to 8 pN, which determines a free energy landscape with two barriers and a transient intermediate state between them along one transition pathway. Our results provide a new insight on protein folding mechanism of two-state proteins.
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