Issue 8, 2007

High-throughput screening of holoprotein conformational stability by dynamic ligand exchange-affinity capillary electrophoresis

Abstract

Dynamic ligand exchange-affinity capillary electrophoresis (DLE-ACE) is introduced as a convenient platform for assessing the conformational stability and relative affinity of a holoprotein to different ligands without off-line sample pretreatment, since ligand exchange and protein unfolding processes are integrated in-capillary during electromigration.

Graphical abstract: High-throughput screening of holoprotein conformational stability by dynamic ligand exchange-affinity capillary electrophoresis

Article information

Article type
Communication
Submitted
11 Apr 2007
Accepted
04 Jun 2007
First published
12 Jun 2007

Analyst, 2007,132, 741-744

High-throughput screening of holoprotein conformational stability by dynamic ligand exchange-affinity capillary electrophoresis

G. Seguí-Lines, J. M. A. Gavina, J. C. D'Amaral and P. Britz-McKibbin, Analyst, 2007, 132, 741 DOI: 10.1039/B705469F

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