AI Article Synopsis
- Engineered bi-histidine (biHis) can improve the mechanical stability of proteins through metal chelation, as shown in the study of protein GB1's mutant G6-53.
- The binding of cobalt ion (Co²⁺) increases mechanical stability marginally, whereas cobalt complex (Co) has a significantly stronger impact.
- This difference arises from the varying thermodynamic stability and kinetic lability of Co and Co complexes, highlighting new opportunities for optimizing protein properties.
Article 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 Co/Co on the mechanical stability of an engineered biHis mutant of protein GB1, G6-53. We found that the binding of Co/Co can lead to an enhancement of the mechanical stability of G6-53, but the degree of enhancement is drastically different. The binding of Co can only lead to marginal enhancement of G6-53's mechanical stability, while Co has a much stronger effect. This large difference is likely due to the large difference in thermodynamic stability and kinetic lability of Co and Co complexes. These results opened up new avenues towards fine tuning the mechanical properties of proteins.
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| http://dx.doi.org/10.1039/c9nr06912g | DOI Listing |
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