Summary
Structural transitions in oligomeric proteins due to ligand binding are important in biomolecular regulatory processes. The transitions may occur on the secondary, tertiary or quarternary structure levels. Detailed consideration of the time sequence of ligand binding to the oligomer shows that there is an intrinsic dynamic asymmetry in all oligomer transitions, even if the initial and the final state are completely symmetric. This asymmetry has important bearing on the evolution and the divergence of the primary structure (amino acid sequence) of oligomeric proteins. It may explain (at least in part) the occurence of oligomeric proteins with similar but not identical protomers. Certain specific groups of oligomers are shown to be under greater evolutionary pressure for protomer structure divergence. The dynamic asymmetry of oligomer transitions also results in higher complexity in reaction kinetics. Some implications on ribosome structural evolution are discussed.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Crane,H.R. (1950). Scient.Monthly, 70, 376
Haselkorn,R., Rothman-Denes,L.B. (1973). Ann.Rev.Biochem.42, 397
Kilkson,R. (1966). J.Theoret.Biol.13, 357
Kilkson,R. (1968). Quart.Rev.Biophys.1, 265
Koshland,D.E., Nemethy,G., Filmer,D. (1966). Biochemistry 5, 365
Monod,J., Wyman,J., Changeux,J.-P. (1965). J.Mol.Biol.12, 88
Thammana,P., Kurland,C.G., Deusser,E., Weber,J., Maschler,R., Stöffler, G., Wittmann,H.G. (1973). Nature, New Biology 242, 47
Woese,C. (1970). Nature 226, 819
Woese,C.R. (1971). J.Theor.Biol.33, 29
Woese,C.R. (1973). Naturwissenschaften 60, 447
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kilkson, R. Intrinsic asymmetry of oligomer transitions and biomolecular evolution. J Mol Evol 5, 125–130 (1975). https://doi.org/10.1007/BF01732517
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF01732517