期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：3
页码：830-833
DOI：10.1073/pnas.70.3.830
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
