Abstract
Random-coiled conformations of fractionated poly(N5-2-hydroxyethyl-L-glutamine) were experimentally investigated and the characteristic ratio was obtained by the Stockmayer–Fixman equation with the experimental results for intrinsic viscosity and weight-averaged molecular weight. Moreover, random-coiled conformations of poly(L-glutamine) and poly(L-glutamic acid) were theoretically analyzed by conformational energy calculations based on intra-residue interactions, and the calculated characteristic ratio was in good agreement with the experimental results.
Similar content being viewed by others
Article PDF
References
D. A. Brant and P. J. Flory, J. Am. Chem. Soc., 87, 2791 (1965).
D. A. Brant, W. G. Miller, and P. J. Flory, J. Mol. Biol., 23, 47 (1967).
P. Doty, J. H. Bradbury, and A. M. Holtzer, J. Am. Chem. Soc., 78, 947 (1956).
D. A. Brant and P. J. Flory, J. Am. Chem. Soc., 87, 2788 (1965).
W. G. Miller, D. A. Brant, and P. J. Flory, J. Mol. Biol., 23, 67 (1967).
H. Fujita, A. Teramoto, T. Yamashita, K. Okita, and S. Ikeda, Biopolymers, 4, 781 (1966).
M. Terbojevich, E. Peggion, A. Cosani, G. D’Este, and E. Scoffone, Eur. Polym. J., 3, 681 (1967).
T. Norisuye, thesis, Osaka University (1973).
F. Heltz, E. Marchal, and G. Spach, Macromolecules, 8, 145 (1975).
S. Tanaka and A. Nakajima, Bull. Inst. Chem. Res., Kyoto Univ., 54, 229 (1976).
G.-W. Chen, thesis, Kyoto University (1981).
M. Miyake, S. Akita, A. Teramoto, T. Norisuye, and H. Fujita, Biopolymers, 13, 1173 (1974).
W. L. Mattice and J.-T. Lo, Macromolecules, 5, 734 (1972).
P. J. Flory, “Principle of Polymer Chemistry,” Cornell University Press, Ithaca, N.Y., 1953.
H. Yamakawa, “Modern Theory of Polymer Solutions,” Harper & Row, New York, 1972.
A. Teramoto and H. Fujita, Adv. Polym. Sci., 18, 65 (1975).
A. Teramoto and H. Fujita, J. Macromol. Sci., C, 15, 165 (1976).
W. H. Stockmayer and M. Fixman, J. Polym. Sci., C, 1, 137 (1963).
T. A. Orofino and P. J. Flory, J. Chem. Phys., 26, 1067 (1957).
T. A. Orofino and P. J. Flory, J. Phys. Chem., 63, 283 (1959).
P. J. Flory and T. G. Fox, J. Am. Chem. Soc., 73, 1904 (1951).
S. Tanaka and A. Nakajima, Polym. J., 2, 717 (1971).
M. Oka and A. Nakajima, Polym. J., 16, 693 (1984). This paper is referenced as paper I.
J. P. Vollmer and G. Spach, Biopolymers, 5, 337 (1967).
E. R. Blout and R. H. Karlson, J. Am. Chem. Soc., 78, 941 (1956).
N. Lupu-Lotan, A. Yaron, A. Berger, and M. Sela, Biopolymers, 3, 625 (1965).
W. Moffitt and J. T. Yang, Proc. Natl. Acad. Sci. U.S.A., 42, 596 (1956).
IUPAC-IUB Commission on Biological Nomenclature, Biochemistry, 9, 3471 (1970).
F. A. Momany, R. F. McGuire, A. W. Burgess, and H. A. Scheraga, J. Phys. Chem., 79, 2361 (1975).
E. Benedetti, C. Pedone, C. Toniolo, G. Nemethy, M. S. Pottle, and H. A. Scheraga, Int. J. Peptide Protein Res., 16, 156 (1980).
G. Nemethy, M. S. Pottle, and H. A. Scheraga, J. Phys. Chem., 87, 1883 (1983).
S. S. Zimmerman, M. S. Pottle, G. Nemethy, and H. A. Scheraga, Macromolecules, 10, 1 (1977).
Equation 1 in the previous paper (paper I) is abbreviated as eq I-1, and so on.
The value l=3.78 Å of ECEPP is slightly smaller than the conventional value 3.8 Å used in the experimental analysis. The effect of this difference on the characteristic ratio being negligibly small (less than 1%), the conventional value 3.8 Å were used in experimental evaluation of ‹R2›0.∞/nl2 by eq 3.
A. Teramoto, private communication.
a=0.35 is more compatible to Figure 2 of ref 13 than a=0.55 which mentioned in ref 13.
The value 8.2 in Table III is recalculated from the original data of ref 8 using Φ0=2.5×1021.
I. D. Rae, S. J. Leach, E. M. Minasian, J. A. Smith, S. S. Zimmerman, J. A. Weigold, Z. I. Hodes, G. Nemethy, R. W. Woody, and H. A. Scheraga, Int. J. Peptide Protein Res., 17, 575 (1981).
M. Oka, G. T. Montelione, and H. A. Scheraga, J. Am. Chem. Soc., 106, 7959 (1984).
M. Oka and A. Nakajima, to be submitted to Polym. J.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Oka, M., Hayashi, T. & Nakajima, A. Random-Coiled Conformation of Polypeptide Chains II. Experimentally Evaluated Characteristic Ratio of Poly(N5-2-hydroxyethyl-L-glutamine) and Theoretical Conformational Analysis of Poly(L-glutamine) and Poly(L-glutamic acid). Polym J 17, 621–631 (1985). https://doi.org/10.1295/polymj.17.621
Issue Date:
DOI: https://doi.org/10.1295/polymj.17.621
Keywords
This article is cited by
-
Association behavior of one-end hydrophobically modified poly[N 5-(2-hydroxyethyl) l-glutamine] in water/ethylene glycol mixed solvent
Colloid and Polymer Science (2007)
-
Theoretical conformational analysis on elastin analogue tetrapeptide Ac-Ala-Pro-Gly-Gly-NHMe
Polymer Bulletin (1991)
-
Theoretical conformational analysis of poly(val-pro-gly-gly) with cis peptide bond at val-pro portion
Polymer Bulletin (1991)
-
Random-coiled conformation of polypeptide chains
Polymer Bulletin (1989)
-
Random-coiled conformation of polypeptide chains
Polymer Bulletin (1989)