Chapter 8. Chemical Modification Strategies for Structure-Function Studies

  1. Michael W. Quick Ph.D.
  1. Gary Rudnick

Published Online: 19 MAR 2003

DOI: 10.1002/0471434043.ch8

Transmembrane Transporters

Transmembrane Transporters

How to Cite

Rudnick, G. (2002) Chemical Modification Strategies for Structure-Function Studies, in Transmembrane Transporters (ed M. W. Quick), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/0471434043.ch8

Editor Information

  1. Department of Neurobiology, University of Alabama at Birmingham School of Medicine, Birmingham, AL, USA

Author Information

  1. Department of Pharmacology, Yale University School of Medicine, New Haven, CT, USA

Publication History

  1. Published Online: 19 MAR 2003
  2. Published Print: 23 AUG 2002

Book Series:

  1. Receptor Biochemistry and Methodology

Book Series Editors:

  1. David R. Sibley

Series Editor Information

  1. Molecular Neuropharmacology Section, Experimental Therapeutics Branch, NINDS, National Institutes of Health, Bethesda, Maryland, USA

ISBN Information

Print ISBN: 9780471065135

Online ISBN: 9780471434047



  • inactivation;
  • labeling;
  • topology;
  • binding site;
  • structure;
  • mechanism;
  • methanethiosulfonate


Transporters are polytopic membrane proteins that allow substrates to move across the lipid bilayer. In this process, the protein undergoes conformational changes that involve internal, external, and transmembrane domains. These conformational changes change the accessibility of the substrate binding site from the internal and external faces of the membrane. The technique of chemical modification has been valuable in understanding which residues in a transporter protein are associated with internal and external loops and transmembrane domains. The modification of reactive residues, such as cysteine, also has provided information about the binding sites for substrates and other ligands for these transporters.