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：1975
卷号：72
期号：12
页码：4933-4935
DOI：10.1073/pnas.72.12.4933
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Our previous introduction of transition dipole coupling helped to explain the splittings in the Amide I modes of antiparallel chain pleated sheet polyglycine I. This mechanism has now been applied to the more likely rippled sheet structure of this polypeptide as well as to the pleated sheet structure of poly(L-alanine). A satisfactorily consistent explanation of the splittings in both polypeptides is obtained. Since a previously incorporated interaction constant has not been used in the present treatment, these results show that transition dipole coupling alone can provide the physical basis for understanding these splittings. It is therefore now possible to predict with confidence the hitherto unidentified v({pi
关键词：vibrational spectra ; normal vibration analysis ; intermolecular interactions ; protein structure
