Abstract
The energies of oligopeptide segments of lysozyme are minimized with respect to the dihedral angles of the central residue. As the length of the oligopeptide segment increases, up to a nonapeptide, the low-energy conformation becomes that observed in the x-ray structure in most cases. This finding suggests that, while short-range interactions appear to play the dominant role in determining the conformation of an amino-acid residue in a protein, the additional interactions required to stabilize the conformation uniquely may be only of medium range, i.e., those within a nonapeptide, and longer-range interactions may be of considerably less importance.
Keywords: short-range interactions, egg-white lysozyme, oligopeptide conformation, protein conformation
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Selected References
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- Sasisekharan V., Ponnuswamy P. K. Studies on the conformation of amino acids. X. Conformations of norvalyl, leucyl and aromatic side groups in a dipeptide unit. Biopolymers. 1971;10(3):583–592. doi: 10.1002/bip.360100312. [DOI] [PubMed] [Google Scholar]