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The coil to globule transition of the polypeptide chain is the physicalphenomenon behind the folding of globular proteins. Globular proteins with asingle domain usually consist of about 30 to 100 amino acid residues, and thisfinite size extends the transition interval of the coil-globule phasetransition. Based on the pedantic derivation of the two-state model, weintroduce the number of amino acid residues of a polypeptide chain as aparameter in the expressions for two cooperativity measures and reveal theirphysical significance. We conclude that the $k_2$ measure, related to thedegeneracy of the denatured state, describes the number of cooperative unitsinvolved in the transition; additionally is found that the famous condition$k_2=1$ is just the necessary condition to classify the protein as thetwo-state folder. We also find that $\Omega_c$ is simply proportional to thesquare of the transition interval. This fact allows us to perform the classicalsize scaling analysis of the coil-globule phase transition. Moreover, these twomeasures are shown to describe different characteristics of protein folding.

The finite size effects and the two-state paradigm of protein folding