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. 1988 Jan 1;249(1):305–308. doi: 10.1042/bj2490305

Suppression of fluorescence of tryptophan residues in proteins by replacement with 4-fluorotryptophan.

P M Bronskill 1, J T Wong 1
PMCID: PMC1148699  PMID: 3124823

Abstract

The tryptophan-auxotrophic Bacillus subtilis LC33 mutant strain utilizes either tryptophan or 4-fluorotryptophan for growth. Proteins therefore could be isolated from these cells in either tryptophan-containing or 4-fluorotryptophan-containing forms. Since 4-fluorotryptophan is non-fluorescent, tryptophan fluorescence would be suppressed in the 4-fluorotryptophan-containing proteins, facilitating the investigation of other chromophores either on the proteins or interacting with the proteins. This approach, potentially applicable to any protein endogenous to or clonable into B. subtilis, was illustrated by an examination of the fluorescence of B. subtilis ribosomal proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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