Abstract
The evaluation of the configurational partition function of a polypeptide molecule, with the internal rotation angles as variables, leads to an improved treatment of the phenomenon of helix-coil transition in polypeptide molecules. The conditional probabilities of occurrence of helical and coiled states of the peptide units are obtained in the form of a 3×3 matrix. The order of this matrix is the lowest possible for the model employed, and is derived by a logical procedure which serves to eliminate redundancies in the enumeration of states. The eigenvalues of this matrix yield the various molecular averages as functions of the degree of polymerization, temperature, and molecular constants. Explicit formulas are given for the degree of intramolecular hydrogen bonding, average number of helical sequences, and the distribution of their lengths, as well as the number average and the weight average of these lengths.
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