King, G. (Gavin) and Dixon, Ann M. (2008) Membrane protein structure : techniques. In: Wiley Encyclopedia of Chemical Biology. Hoboken, N.J.: John Wiley & Sons. ISBN 9780471754770

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Abstract

The biological importance of membrane proteins has been recognized worldwide for many years, but historically these proteins have proved difficult to characterize structurally because of a variety of experimental challenges. Recently, technological advances across several disciplines have prompted considerable progress in three-dimensional structure determination of membrane proteins. This review describes the state-of-the-art methods that have successfully produced high-resolution membrane protein structures to date. Most notably, X-ray crystallography will be discussed, as this technique has made by far the largest contribution to our current knowledge of membrane protein structure. This is followed by discussion of nuclear magnetic resonance spectroscopy and cryo-electron microscopy, both techniques that have also been successful in producing high-resolution structures for membrane proteins, albeit to a lesser degree than X-ray crystallography. Finally, we will discuss atomic force microscopy. Although this technique cannot be used for atomic level structural determination, it offers distinct advantages for investigation of membrane protein oligomerization, dynamics, and large-scale conformational changes. Recent notable membrane protein structures are included throughout to illustrate progress in the field as well as the strengths and weaknesses of each method.

Item Type:	Book Item
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Membrane proteins
Publisher:	John Wiley & Sons
Place of Publication:	Hoboken, N.J.
ISBN:	9780471754770
Book Title:	Wiley Encyclopedia of Chemical Biology
Date:	2008
Identification Number:	10.1002/9780470048672.wecb653
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
URI:	http://wrap.warwick.ac.uk/id/eprint/40213

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