AI Article Synopsis
- A new disulfide bond (Cys46-Cys61) was engineered in the heme region of myoglobin to influence the protein's shape and activity.
- The modification's effects were validated through various techniques, including X-ray crystallography and kinetic UV-vis studies.
- The results indicate that this design closely mirrors the structural and functional properties of native human neuroglobin.
Article Abstract
An artificial disulfide bond (Cys46-Cys61) was designed in the heme distal site of myoglobin, which regulates the conformation of the heme distal His64 and the protein reactivity, as confirmed by X-ray crystallography, EPR, and kinetic UV-vis studies. This study shows the successful design of a disulfide bond with suitable positions in globins, conferring a structure and function like those of the native human neuroglobin.
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| http://dx.doi.org/10.1039/d2cc01753a | DOI Listing |
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