Unit

UNIT 4.15 The Substituted-Cysteine Accessibility Method (SCAM) to Elucidate Membrane Protein Structure

  1. George Liapakis,
  2. Merrill M. Simpson,
  3. Jonathan A. Javitch

Published Online: 1 MAY 2001

DOI: 10.1002/0471142301.ns0415s08

Current Protocols in Neuroscience

Current Protocols in Neuroscience

How to Cite

Liapakis, G., Simpson, M. M. and Javitch, J. A. 2001. The Substituted-Cysteine Accessibility Method (SCAM) to Elucidate Membrane Protein Structure. Current Protocols in Neuroscience. 8:4.15:4.15.1–4.15.10.

Author Information

  1. Columbia University, New York, New York

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: AUG 1999

Abstract

The substituted-cysteine accessibility method (SCAM) provides an approach to identifying the residues in the membrane-spanning segments that line a channel, transporter, or binding-site crevice. SCAM can also be used to determine differences in the structures of the membrane-spanning segments in different functional states of the proteins, to map electrostatic potential in the membrane-spanning domains, and to size a channel or binding-site crevice. The protocol in this unit describes the use of SCAM to map the binding-site crevice of a G-protein coupled receptor (GPCR) which binds ligand within the transmembrane portion of the receptor.