Abstract
A succession of apparent local energy minima, in which the energies decrease successively, have been located for deca-L-alanine and the octapeptide loop of ribonuclease. The lowest energy minima were approximately 40 kcal/mole lower than the highest ones. The results suggest that the computational methods used here might be of considerable use in searching for the global energy minimum of larger polypeptides.
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Selected References
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- Edsall J. T., Flory P. J., Kendrew J. C., Liquori A. M., Nemethy G., Ramachandran G. N., Scheraga H. A. A proposal of standard conventions and nomenclature for the description of polypeptide conformation. J Biol Chem. 1966 Feb 25;241(4):1004–1008. [PubMed] [Google Scholar]
- Gibson K. D., Scheraga H. A. Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide. Proc Natl Acad Sci U S A. 1967 Aug;58(2):420–427. doi: 10.1073/pnas.58.2.420. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kotelchuck D., Scheraga H. A. The influence of short-range interactions on protein conformation. I. Side chain-backbone interactions within a single peptide unit. Proc Natl Acad Sci U S A. 1968 Dec;61(4):1163–1170. doi: 10.1073/pnas.61.4.1163. [DOI] [PMC free article] [PubMed] [Google Scholar]