Associated Papers
The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation.
McClelland LJ et al.
Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry, 2015
Structural basis for cytochrome c Y67H mutant to function as a peroxidase.
Lan W et al.
Plos One, 2014
Insights into the role of the histidines in the structure and stability of cytochrome c.
Sinibaldi F et al.
Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry, 2006
Structure, function, and temperature sensitivity of directed, random mutants at proline 76 and glycine 77 in omega-loop D of yeast iso-1-cytochrome c.
Fetrow JS et al.
Biochemistry, 1998
Loop replacement and random mutagenesis of omega-loop D, residues 70-84, in iso-1-cytochrome c.
Mulligan-Pullyblank P et al.
The Journal of Biological Chemistry, 1996
Mutations of iso-1-cytochrome c at positions 13 and 90. Separate effects on physical and functional properties.
Huang Y et al.
European Journal of Biochemistry, 1994
Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix.
Fredericks ZL et al.
Biochemistry, 1993
Temperature-sensitive variants of Saccharomyces cerevisiae iso-1-cytochrome c produced by random mutagenesis of codons 43 to 54.
Wang XH et al.
Journal of Molecular Biology, 1991
The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector.
Hilgen SE et al.
Protein Engineering, 1991
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