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- W2964377961 abstract "Abstract Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X‐ray structure of perdeuterated high‐potential iron‐sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high‐resolution neutron crystallography." @default.
- W2964377961 created "2019-08-13" @default.
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- W2964377961 creator A5043399309 @default.
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- W2964377961 date "2019-08-10" @default.
- W2964377961 modified "2023-10-02" @default.
- W2964377961 title "Characterization of perdeuterated high‐potential iron‐sulfur protein with high‐resolution X‐ray crystallography" @default.
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- W2964377961 doi "https://doi.org/10.1002/prot.25793" @default.
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