T4 phage lysozyme. A protein designed for understanding trypotphan photophysics

Bruce Hudson, Danni Harris

Research output: Chapter in Book/Report/Conference proceedingConference contribution

4 Scopus citations

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has been genetically engineered to prepare all possible variants in which one or more of the tryptophan residue have been replaced by tyrosine.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.

Original languageEnglish (US)
Title of host publicationProceedings of SPIE - The International Society for Optical Engineering
EditorsJoseph F. Lakowicz
PublisherPubl by Int Soc for Optical Engineering
Pages80-91
Number of pages12
ISBN (Print)0819402451
StatePublished - Dec 1 1990
EventTime-Resolved Laser Spectroscopy in Biochemistry II - Los Angeles, CA, USA
Duration: Jan 15 1990Jan 17 1990

Publication series

NameProceedings of SPIE - The International Society for Optical Engineering
Volume1204 pt 1
ISSN (Print)0277-786X

Other

OtherTime-Resolved Laser Spectroscopy in Biochemistry II
CityLos Angeles, CA, USA
Period1/15/901/17/90

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Computer Science Applications
  • Applied Mathematics
  • Electrical and Electronic Engineering

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  • Cite this

    Hudson, B., & Harris, D. (1990). T4 phage lysozyme. A protein designed for understanding trypotphan photophysics. In J. F. Lakowicz (Ed.), Proceedings of SPIE - The International Society for Optical Engineering (pp. 80-91). (Proceedings of SPIE - The International Society for Optical Engineering; Vol. 1204 pt 1). Publ by Int Soc for Optical Engineering.