Probing protein folding with substitution-inert metal ions. Folding kinetics of cobalt(III)-cytochrome c [13]

Journal of the American Chemical Society

Volumn 121, Issue 50, 1999, Pages 11918-11919

  Tezcan, F Akif ^a   Winkler, Jay R ^a   Gray, Harry B ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT DERIVATIVE; CYTOCHROME C OXIDASE; LIGAND; METAL ION;

CIRCULAR DICHROISM; HORSE; KINETICS; LETTER; PH; PROTEIN FOLDING; THERMODYNAMICS; TUNA; ULTRAVIOLET SPECTROSCOPY;

EID: 0033596332     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja993447k     Document Type: Letter

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18. The folding reaction, which was monitored by UV-visible absorption, CD, and fluorescence spectroscopy, follows biexponential kinetics. The rates and relative amplitudes agree within error for all three methods, although varying degrees of signal change are observed during the mixing deadtime.
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24. Solutions for the UV-vis measurements were equilibrated for 24 h. The pH-titration fits were for a two-species equilibrium in which the species protonate independently. Nevertheless, these fits did not reveal a significant population of a second species in tuna or horse Co-cyt c.
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