Cytochrome c: Occurrence and functions
Article Abstract:
Cytochromes c, are among the most studied proteins, possibly due to their relatively high thermodynamic stability and their red color, which makes protein purification easier and the three-dimensional structure of mitochondrial cytochrome c has been solved in the 1970s.The small size, high solubility, high helical content and the presence of the heme cofactor have allowed mitochondrial and some bacterial cytochromes c to be studied through spectroscopic techniques, which have contributed to making cytochrome c a very popular protein among biochemist and biophysicists.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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Protein folding thermodynamics and dynamics: Where physics, chemistry and biology meet
Article Abstract:
A summary of basic questions and simple, coarse-grained methods is presented that provide a basis for a fundamental understanding of protein folding thermodynamics and kinetics. A discussion is also presented on detailed studies of folding mechanisms of specific proteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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A statistical thermodynamic model of the protein ensemble
Article Abstract:
The background, physical basis and the experimental validation of a structural thermodynamic model of protein ensemble, known as COREX is reviewed. The COREX model reproduces a surprising number of apparently disparate biophysical and functional properties of proteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2006
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