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Updated: Sep 25, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Structural and functional regulations by a disulfide bond designed in myoglobin like human neuroglobin
Li-Juan Sun1, Hong Yuan2, Lu Yu3
1Hengyang Medical College, University of South China, Hengyang 421001, China. ywlin@usc.edu.cn.
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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