Abstract
Semi-empirical energy calculations were performed to determine the conformation of the α-helix—random coil—α-helix polypeptide. The random-coil region includes only one amino acid residue in these calculations. The results are illustrated by conformational energy maps. The results indicate that the conformation of the structures is not uniquely determined, but the dihedral angles of the residue in the random region are significantly restricted.
Similar content being viewed by others
Article PDF
References
H. A. Scheraga, S. J. Leach, R. A. Scott, and G. Nemethy, Discuss. Faraday Soc., 40, 268 (1965).
P. Y. Chou and G. D. Fasman, Biochemistry, 13, 222 (1974).
K. Nagano, J. Mol. Biol., 75, 401 (1973).
O. B. Ptitsyn and A. A. Rashin, Dokl. Acad. Nauk SSSR, 213, 473 (1973).
M. G. Rossman and A. Liljas, J. Mol. Biol., 85, 177 (1974).
T. Ooi, R. A. Scott, G. Vanderkooi, and H.A. Scheraga, J. Chem. Phys., 46, 4410 (1967).
D. Poland and H. A. Scheraga, Biochemistry, 6, 3791 (1967).
H. A. Scheraga, “Adv. Phys. Org. Chem.,” Academic Press, New York, N.Y., 1968, p 103.
IUPAC—IUB Commission on Biochemical Nomenclature (1970), Biochemistry, 9, 3471.
H. C. Watson, Progr. Stereochem., 4, 299 (1969).
P. K. Ponnuswamy, P. K. Warme, and H. A. Scheraga, Proc. Nat. Acad. Sci. USA, 70, 830 (1973).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Nakata, Y., Suzuki, K. Conformation of the Helix—Coil—Helix Polypeptide. Polym J 7, 444–448 (1975). https://doi.org/10.1295/polymj.7.444
Issue Date:
DOI: https://doi.org/10.1295/polymj.7.444