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Finite size effects on the cooperative thermal denaturation of proteins areconsidered. A dimensionless measure of cooperativity, Omega, scales as N^zeta,where N is the number of amino acids. Surprisingly, we find that zeta isuniversal with zeta = 1 + gamma, where the exponent gamma characterizes thedivergence of the susceptibility for a self-avoiding walk. Our lattice modelsimulations and experimental data are consistent with the theory. Our findingrationalizes the marginal stability of proteins and substantiates the earlierpredictions that the efficient folding of two-state proteins requires thefolding transition temperature to be close to the collapse temperature.Comment: 3 figures. Physical Review Letters (in press

Finite Size Effects on Thermal Denaturation of Globular Proteins