Article
Thermodynamic Control of Domain Swapping by Modulating the Helical Propensity in the Hinge Region of Myoglobin.
Chemistry, an Asian journal - 2 Jun 2020
Nagao Satoshi, Suda Ayaka, Kobayashi Hisashi, Shibata Naoki, Higuchi Yoshiki, Hirota Shun
Abstract excerpt
Domain swapping is an exception to Anfinsen's dogma, and more than one structure can be produced from the same amino acid sequence by domain swapping. We have previously shown that myoglobin (Mb) can form a domain-swapped dimer in which the hinge region is converted to a helical structure. In this study, we showed that domain-swapped dimerization of Mb was achieved by a single Ala mutation of Gly at position 80....
Topics
- Crystallography, X-Ray
- Escherichia coli
- Models, Molecular
- Mutation
- Myoglobin
- Protein Conformation
- Thermodynamics