Kinetics of unfolding and folding of horse heart ferricytochrome c with urea.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Inorganic Biochemistry;Harbury,1973
2. [16] Circular dichroism spectroscopy of hemoproteins
3. Conformation of cytochromes. III. Effect of urea, temperature, extrinsic ligands, and pH variation on the conformation of horse heart ferricytochrome c
4. Equilibrium and kinetic studies of unfolding of homologous cytochromes c.
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1. Cytochromecon Silica Nanoparticles: Influence of Nanoparticle Size on Protein Structure, Stability, and Activity;Small;2009-02-20
2. The barriers in protein folding;Nature Structural Biology;1994-03
3. Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71;Biochemistry;1986-11-04
4. An electrochemical study of the stability of cytochrome c3 from Desulfovibrio desulfuricans Norway strain;Bioelectrochemistry and Bioenergetics;1986-02
5. Effect of methyl viologen on the electrochemical behavior of denatured cytochrome c at mercury and solid electrodes;Journal of Electroanalytical Chemistry and Interfacial Electrochemistry;1985-03
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