Issue 20, 2011

A small fluorophore reporter of protein conformation and redox state

Abstract

A new thiol-specific reagent introduces a small bis(methylamino)terephthalic acid fluorophore into proteins. The noninvasive probe with distinct spectroscopic properties offers many advantages for protein labeling, purification, and mechanistic work promising to serve as a powerful tool in studies of protein folding and heme redox reactions.

Graphical abstract: A small fluorophore reporter of protein conformation and redox state

Supplementary files

Article information

Article type
Communication
Submitted
15 Feb 2011
Accepted
14 Mar 2011
First published
12 Apr 2011

Chem. Commun., 2011,47, 5714-5716

A small fluorophore reporter of protein conformation and redox state

G. J. Pound, A. A. Pletnev, X. Fang and E. V. Pletneva, Chem. Commun., 2011, 47, 5714 DOI: 10.1039/C1CC10896D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements