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Issue 42, 2019
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Single molecule force spectroscopy reveals that the oxidation state of cobalt ions plays an important role in enhancing the mechanical stability of proteins

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Abstract

Engineered bi-histidine (biHis)-based metal chelation is a general and robust method to enhance the mechanical stability of proteins. Here we used single molecule force spectroscopy techniques to investigate the effect of binding of Co2+/Co3+ on the mechanical stability of an engineered biHis mutant of protein GB1, G6-53. We found that the binding of Co2+/Co3+ can lead to an enhancement of the mechanical stability of G6-53, but the degree of enhancement is drastically different. The binding of Co2+ can only lead to marginal enhancement of G6-53's mechanical stability, while Co3+ has a much stronger effect. This large difference is likely due to the large difference in thermodynamic stability and kinetic lability of Co2+ and Co3+ complexes. These results opened up new avenues towards fine tuning the mechanical properties of proteins.

Graphical abstract: Single molecule force spectroscopy reveals that the oxidation state of cobalt ions plays an important role in enhancing the mechanical stability of proteins

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Article information


Submitted
11 Aug 2019
Accepted
16 Sep 2019
First published
04 Oct 2019

Nanoscale, 2019,11, 19791-19796
Article type
Paper

Single molecule force spectroscopy reveals that the oxidation state of cobalt ions plays an important role in enhancing the mechanical stability of proteins

J. Xia, J. Zuo and H. Li, Nanoscale, 2019, 11, 19791
DOI: 10.1039/C9NR06912G

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