Abstract
The aromatic amino acid, tryptophan, was studied with the semiempirical self-consistent-field method. Ground-state bond lengths and π-election charge densities as well as the energies and transition moment directions for the first three absorption transitions were calculated. Published experimental work indicates that the indole part of tryptophan may enter into excited state interactions with neighboring solvent molecules; since this interaction will lead to emissive properties different from those of absorption, the present work includes a calculation of the transition moment direction for light emission by tryptophan.
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Selected References
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- BEAVEN G. H., HOLIDAY E. R. Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem. 1952;7:319–386. doi: 10.1016/s0065-3233(08)60022-4. [DOI] [PubMed] [Google Scholar]
- Lynn J., Fasman G. D. Conformational dependence of fluorescence polarization spectra of L-tryptophan containing copolypeptides. Biopolymers. 1968;6(1):159–163. doi: 10.1002/bip.1968.360060114. [DOI] [PubMed] [Google Scholar]
- WEBER G. Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds. Biochem J. 1960 May;75:335–345. doi: 10.1042/bj0750335. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walker M. S., Bednar T. W., Lumry R. Exciplex formation in the excited state of indole. J Chem Phys. 1966 Nov 1;45(9):3455–3456. doi: 10.1063/1.1728133. [DOI] [PubMed] [Google Scholar]
- Yeargers E., Augenstein L. Vacuum ultraviolet studies on the nature of the radiation inactivation of trypsin. Biophys J. 1968 Apr;8(4):500–509. doi: 10.1016/S0006-3495(68)86503-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
