Acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00678a031
Reference34 articles.
1. Evidence for Residual Structure in Acid- and Heat-denatured Proteins
2. The Structure of the Heme Crevice of Ferric Cytochrome c Alkylated at Methionine-80
3. The existence of heme-protein coordinate-covalent bonds in denaturing solvents
4. Participation of the protein ligands in the folding of cytochrome c
5. On the compounds of ferricytochrome C appearing in acid solution
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2. Uncovering dehydration in cytochrome c refolding from urea- and guanidine hydrochloride-denatured unfolded state by high pressure spectroscopy;Biophysics and Physicobiology;2019
3. Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c;Biochemistry;2017-12-08
4. Non-two-state thermal denaturation of ferricytochrome c at neutral and slightly acidic pH values;Biophysical Chemistry;2015-08
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