1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb17582.x/fullpdf
Reference28 articles.
1. 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states
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5. Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c
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