@inproceedings{7403c50ea99145a89987ee26f81bc3a9,
title = "T4 phage lysozyme. A protein designed for understanding trypotphan photophysics",
abstract = "Bacteriophage T4 lysozyme in its wild type form contains three tryptophan residues (at sequence positions 126, 138 and 158). These three residues are in rather different evironments in the proteins: 126 and 158 are near the protein surface while residue 138 is more buried. T4 lysozyme has been genetically engineered to prepare all possible variants in which one or more of the tryptophan residue have been replaced by tyrosine. The available data supports the hypothesis that this substitution has, at most, a very minor effect on the structure of the protein.",
author = "Bruce Hudson and Danni Harris",
year = "1990",
language = "English (US)",
isbn = "0819402451",
series = "Proceedings of SPIE - The International Society for Optical Engineering",
publisher = "Publ by Int Soc for Optical Engineering",
pages = "80--91",
editor = "Lakowicz, {Joseph F.}",
booktitle = "Proceedings of SPIE - The International Society for Optical Engineering",
note = "Time-Resolved Laser Spectroscopy in Biochemistry II ; Conference date: 15-01-1990 Through 17-01-1990",
}