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.

Cytochrome c

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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.

Analysis, Protein folding

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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.

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