Comparison of the Conformational Stability of the Molten Globule and Native States of Horse Cytochrome c

1994 ◽  
Vol 237 (3) ◽  
pp. 336-348 ◽  
Author(s):  
Yoshihisa Hagihara ◽  
Yukihiro Tan ◽  
Yuji Goto
Keyword(s):  
Cytochrome C ◽  
Molten Globule ◽  
Conformational Stability ◽  
Horse Cytochrome

Conformational Fluctuation of Native-Like and Molten-Globule-Like Cytochrome c Observed by Time-Resolved Hole Burning†

Biochemistry ◽  
1999 ◽  
Vol 38 (6) ◽  
pp. 1802-1810 ◽  
Author(s):  
Yutaka Shibata ◽  
Hirokazu Takahashi ◽  
Rina Kaneko ◽  
Atusi Kurita ◽  
Takashi Kushida
Keyword(s):  
Cytochrome C ◽  
Molten Globule ◽  
Hole Burning ◽  
Time Resolved ◽  
Conformational Fluctuation

scholarly journals The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T

1984 ◽  
Vol 217 (3) ◽  
pp. 595-599 ◽  
Author(s):  
C J A Wallace
Keyword(s):  
Structural Change ◽  
Cytochrome C ◽  
Oxygen Uptake ◽  
Redox Potential ◽  
Biological Properties ◽  
Amino Groups ◽  
Cytochromes C ◽  
Restricted Region ◽  
Horse Cytochrome

The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.

Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

2015 ◽  
Vol 585 ◽  
pp. 52-63 ◽  
Author(s):  
Rishu Jain ◽  
Rajesh Kumar ◽  
Sandeep Kumar ◽  
Ritika Chhabra ◽  
Mukesh Chand Agarwal ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Folding Kinetics ◽  
Ph Dependent ◽  
Kinetics Of ◽  
Horse Cytochrome
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