Theory of the Far-Ultraviolet Spectrum of Polypeptides in the β Conformation
Authors:
- 15 January 1967
- journal article
- research article
- Published by AIP Publishing in The Journal of Chemical Physics
- Vol. 46 (2) , 532-536
Abstract
The electronic excited states in polypeptides of the β conformation corresponding to the lowest energy π—π* transition are derived from molecular‐exciton theory. Transition energies are calculated in the monopole—monopole approximation, and the results are compared with polarized film spectra obtained in the present study, as well as with experimental data of other investigators. It appears that either parallel sheets or mixtures of parallel and antiparallel sheets are present in poly‐L‐lysine solutions and films.Keywords
This publication has 13 references indexed in Scilit:
- The optical rotatory properties of the beta-configuration in polypeptides and proteins.Proceedings of the National Academy of Sciences, 1966
- The circular dichroism of the β structure of poly-l-lysineBiochemical and Biophysical Research Communications, 1966
- An X-ray diffraction study of poly-L-lysine hydrochlorideJournal of Molecular Biology, 1965
- On the Singlet-Exciton States of Crystalline AnthraceneThe Journal of Chemical Physics, 1965
- Circular Dichroism Measurements to 185 mμ in a Commercial Recording SpectrophotometerReview of Scientific Instruments, 1965
- Origin of the Cotton Effect of Helical PolypeptidesThe Journal of Chemical Physics, 1962
- THE FAR ULTRAVIOLET ABSORPTION SPECTRA OF POLYPEPTIDE AND PROTEIN SOLUTIONS AND THEIR DEPENDENCE ON CONFORMATIONProceedings of the National Academy of Sciences, 1961
- Space Groups and Their Representations1957
- Pi-Electron Forces between Conjugated Double Bond MoleculesThe Journal of Chemical Physics, 1955
- Two Pleated-Sheet Configurations of Polypeptide Chains Involving Both Cis and Trans Amide GroupsProceedings of the National Academy of Sciences, 1953