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Biophys J. 2011 Feb 16;100(4):1094-9. doi: 10.1016/j.bpj.2011.01.011.

Inhibitor binding increases the mechanical stability of staphylococcal nuclease.

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1
Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung, Taiwan, Republic of China. [corrected]

Erratum in

  • Biophys J. 2011 Mar 16;100(6):1596.

Abstract

Staphylococcal nuclease (SNase) catalyzes the hydrolysis of DNA and RNA in a calcium-dependent fashion. We used AFM-based single-molecule force spectroscopy to investigate the mechanical stability of SNase alone and in its complex with an SNase inhibitor, deoxythymidine 3',5'-bisphosphate. We found that the enzyme unfolds in an all-or-none fashion at ∼26 pN. Upon binding to the inhibitor, the mechanical unfolding forces of the enzyme-inhibitor complex increase to ∼50 pN. This inhibitor-induced increase in the mechanical stability of the enzyme is consistent with the increased thermodynamical stability of the complex over that of SNase. Because of its strong mechanical response to inhibitor binding, SNase, a model protein folding system, offers a unique opportunity for studying the relationship between enzyme mechanics and catalysis.

PMID:
21320455
PMCID:
PMC3037565
DOI:
10.1016/j.bpj.2011.01.011
[Indexed for MEDLINE]
Free PMC Article

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