The fluid-mosaic model of membrane structure formulated by Singer
and Nicolson in the early 1970s has proven to be a durable concept
in terms of the principles governing the organization of the
constituent lipids and proteins. During the past 30 or so years a
great deal of information has accumulated on the composition of
various cell membranes and how this is related to the dif ferent
functions that membranes perform. Nevertheless, the task of
explaining particular functions at the molecular level has been
hampered by lack of struc tural detail at the atomic level. The
reason for this is primarily the difficulty of crystallizing
membrane proteins which require strategies that differ from those
used to crystallize soluble proteins. The unique exception is
bacteriorhodopsin of the purple membrane of Halobacterium halobium
which is interpolated into a membrane that is neither fluid nor in
a mosaic configuration. To date only 50 or so membrane proteins
have been characterised to atomic resolution by diffraction
methods, in contrast to the vast data accumulated on soluble
proteins. Another factor that has been difficult to explain is the
reason why the lipid compliment of membranes is often extremely
complex. Many hundreds of different molecular species of lipid can
be identified in some membranes. Remarkably, the particular
composition of each membrane appears to be main tained within
relatively narrow limits and its identity distinguished from other
morphologically-distinct membranes.
General
Imprint: |
Kluwer Academic / Plenum Publishers
|
Country of origin: |
United States |
Series: |
Subcellular Biochemistry, 37 |
Release date: |
July 2004 |
First published: |
2004 |
Editors: |
Peter J. Quinn
|
Dimensions: |
235 x 155 x 36mm (L x W x T) |
Format: |
Hardcover
|
Pages: |
499 |
Edition: |
2004 ed. |
ISBN-13: |
978-0-306-48425-4 |
Categories: |
Books >
Science & Mathematics >
Biology, life sciences >
Cellular biology >
General
|
LSN: |
0-306-48425-0 |
Barcode: |
9780306484254 |
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