Campus Units

Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

12-1995

Journal or Book Title

Journal of the American Chemical Society

Volume

117

Issue

48

First Page

11850

Last Page

11853

DOI

10.1021/ja00153a005

Abstract

The development of a new intrinsic optical probe of protein structure and dynamics, Nl-methyl-7- azatryptophan (1M7AT), is reported. The utility of this nonnatural amino acid derivative lies in its single-exponential, long-lived fluorescence decay (21.7 f 0.4 ns) and in its high fluorescence quantum yield (0.53 f 0.07). Its absorption and emission maxima are red-shifted 10 and 65 nm, respectively, from those of tryptophan. These characteristics permit its unambiguous detection with unprecedented discrimination against emission from multiply occurring native tryptophan residues. In a mixture of these two amino acids, no tryptophan signal is detected until the tryptophan: N1-methyl-7-azatryptopharna tio exceeds 75: 1. Consequently, NI-methyl-7-azatryptophains ideal for studying the interactions of small peptides containing it with large proteins.

Comments

Reprinted (adapted) with permission from Journal of the American Chemical Society 117 (1995): 11850, doi: 10.1021/ja00153a005. Copyright 1995 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

Included in

Chemistry Commons

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