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：1972
卷号：69
期号：11
页码：3301-3304
DOI：10.1073/pnas.69.11.3301
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Ab initio calculations on di-, tri-, tetra-, and pentapeptides of glycine in various conformations are reported. Hydrogen bonding is observed as an important stabilizing force in [α]-helical conformations. These studies on polypeptides of glycine of reasonable size show for the first time that the forces acting to stabilize polypeptide conformations can be extracted directly from theoretical studies, without prior postulation of their existence or need for concern that neglect or approximation of various integrals may have biased the results.
关键词：hydrogen bonding ; poly(glycine) ; self-consistent field calculations
