Quantum Mechanical Partitioning of the Energies of Polypeptides: Conformational Study of Polyglycine

Authors

Steve Scheiner, Utah State UniversityFollow
C. W. Kern, Ohio State University

Document Type

Article

Journal/Book Title

Journal of the American Chemical Society

Publication Date

11-1978

Publisher

American Chemical Society

Volume

100

Abstract

The total energy of a polypeptide is partitioned into the interaction energies between pairs of residues. The interactions between adjacent residues are evaluated by quantum mechanical methods. An empirical hydrogen bond potential based on the quantum mechanical interaction between amide units is formulated and used to calculate the interaction energy between nonadjacent residues. This treatment is used to study regular helical conformations of an isolated single strand of polyglycine. The a: helix is found most stable while the 3₁₀ and 2₇ helices are also low-energy structures. The calculated results are compared to those obtained via classical partitioning procedures as well as experiment.

Comments

Originally published in the Journal of the American Chemical Society by the American Chemical Society . Publisher’s PDF available through remote link. DOI: 10.1021/ja00492a017

Recommended Citation

Quantum Mechanical Partitioning of the Energies of Polypeptides: Conformational Study of Polyglycine S. Scheiner and C. W. Kern J. Am. Chem. Soc., 1978 100 (24), 7539-7548.