Campus Units

Chemistry, Biochemistry, Biophysics and Molecular Biology

Document Type

Article

Publication Version

Published Version

Publication Date

9-1990

Journal or Book Title

Journal of the American Chemical Society

Volume

112

Issue

20

First Page

7419

Last Page

7421

DOI

10.1021/ja00176a066

Abstract

7-Amtryptophan is an ideal noninvasive in situ probe of protein structure and dynamics and provides an alternative to the use of ,tryptophan. 7-Azatryptophan affords a single-exponential fluorescence decay in aqueous solution, unlike tryptophan. Its absorption and fluorescence spectra are distinguishable from those of tryptophan. Its fluorescence spectrum and lifetime are sensitive to the environment. It can be used in peptide synthesis, and it can be incorporated into bacterial protein. These facts render 7-azatryptophan a unique probe that has the potential for widespread use.

Comments

Reprinted (adapted) with permission from Journal of the American Chemical Society 112 (1990): 7419, doi: 10.1021/ja00176a066. Copyright 1990 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

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