Issue 19, 2003

Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites

Abstract

The binding affinity of aspartate decarboxylase has been probed using MALDI-TOF spectrometry; adducts formed covalently in the active site were detected by MALDI-TOF mass spectrometry after incubation of the enzyme with a range of potential ligands in the presence of NaCNBH3; this has highighted key structural features which will aid design of potential inhibitors.

Graphical abstract: Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites

Supplementary files

Article information

Article type
Communication
Submitted
16 Goue. 2003
Accepted
18 Eost 2003
First published
01 Gwen. 2003

Chem. Commun., 2003, 2416-2417

Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites

M. E. Webb, E. Stephens, A. G. Smith and C. Abell, Chem. Commun., 2003, 2416 DOI: 10.1039/B308182F

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