title: Applicability of broken-rodlike chain model to conformational analysis of polypeptide chain.
abstract: In order to check the applicability of the broken-rodlike (BR) chain model, consisting of several rods alternatively joined by flexible random coils, to the conformational analysis of a polypeptide chain in the helix-to-coil transition regions, two relations predicted by the Zimm and Bragg theory and the method with the BR chain model are compared. It is shown that, despite a clear difference between the models employed in the two methods, they give substantially identical results in both probability P(j) that a helical residue is in a helical sequence j units long and averaged helical fraction dependence of the mean-squared radius of gyration. Thus the use of the method with the BR chain model in the conformational analysis of a polypeptide chain could be rationalized, at least, with the same degree of approximation as is assumed in the Zimm and Bragg theory. Using the scattering function for the BR chain model, averaged helical-sequence lengths are evaluated for partially ionized poly(L-glutamic acid) (PGA) in added-salt aqueous solution and nonionized PGA in N-methylacetamide, both in a helical state. As a result, it is shown that the length in the latter molecule is approximately tenfold longer than that in the former one.
authors.affiliation: Department of Applied Chemistry, School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Muroga
mesh_terms: D003198:Computer Simulation; D008432:Mathematical Computing; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides; D011099:Polyglutamic Acid