Ion Channels
From Atomic Resolution Physiology to Functional Genomics
Published on 19. April 2002
Book
Hardback
288 pages
978-0-470-84375-8 (ISBN)
Description
Ion channels provide a unique opportunity to use computational approaches to attempt an understanding of the function of a membrane protein, starting with an atomic resolution structure and progressing through a hierarchy of theoretical descriptions until one can account quantitatively for their physiological function. This book brings together physiologists, structural biologists and theorists who came together to help define the direction of the field in the immediate future. Topics covered include:
the x-ray structure of channels and pores
computer simulation of channel function
detailed data on potassium channels, chloride and calcium channels, and ligand-gated ion channels
the x-ray structure of channels and pores
computer simulation of channel function
detailed data on potassium channels, chloride and calcium channels, and ligand-gated ion channels
Reviews / Votes
"...I would particularly recommend it to students who wish to gain a flavour of the discussions, disputes and personalities within this field..." (The Biochemist, 31 March 2003)More details
Series
Language
English
Place of publication
New York
United States
Target group
College/higher education
Professional and scholarly
Dimensions
Height: 239 mm
Width: 157 mm
Thickness: 18 mm
Weight
567 gr
ISBN-13
978-0-470-84375-8 (9780470843758)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Persons
The Novartis Foundation is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.
Content
Introduction: stretching the envelope in structure-function studies of ion channels (M. Sansom) Structure of acetylcholine-gated channel (N. Unwin)
The 2.7 A structure of AChBP, homologue of the ligand-building domain of the nicotonic acetylcholine receptor (K. Brejc, et al.)
The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice (A. Mitra, et al.)
The structure of Glpf, a glycerol conducting channel (D. Fu, et al.)
Water in ion channels and pores-simulation studies (M. Sansom, et al.)
What can be deduced about the structure of Shaker from available data? (B. Roux)
Permeation energetics in a model potassium channel (S. Garofoli, et al.)
The ? subunit of Kv1 channels: voltage-gated enzyme or safety switch? (J. Gulbis)
EPR approaches to ion channel structure and function (E. Perozo, et al.)
Excitability is mediated by the T1 domain of the voltage-gated potassium channel (S. Choe, et al.)
Structural organization of the voltage sensor in voltage-dependent potassium channels (D. Papazian, et al.)
Electron diffraction of a bacterial CIC -type chloride channel (M. Pirruccello, et al.)
A protein chemical approach to channel structure and function: the proton channel of the vacuolar H+-ATPase (J. Findlay and M. Harrison)
Acetylcholine receptors, between closed and open (A. Auerbach)
Functional genomics of ionotropic acetylcholine receptors in Caenorhabditis elegans and Drosophilia melanogaster (D. Satelle et al.)
Final General Discussion
Index of Contributors
Subject Index
The 2.7 A structure of AChBP, homologue of the ligand-building domain of the nicotonic acetylcholine receptor (K. Brejc, et al.)
The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice (A. Mitra, et al.)
The structure of Glpf, a glycerol conducting channel (D. Fu, et al.)
Water in ion channels and pores-simulation studies (M. Sansom, et al.)
What can be deduced about the structure of Shaker from available data? (B. Roux)
Permeation energetics in a model potassium channel (S. Garofoli, et al.)
The ? subunit of Kv1 channels: voltage-gated enzyme or safety switch? (J. Gulbis)
EPR approaches to ion channel structure and function (E. Perozo, et al.)
Excitability is mediated by the T1 domain of the voltage-gated potassium channel (S. Choe, et al.)
Structural organization of the voltage sensor in voltage-dependent potassium channels (D. Papazian, et al.)
Electron diffraction of a bacterial CIC -type chloride channel (M. Pirruccello, et al.)
A protein chemical approach to channel structure and function: the proton channel of the vacuolar H+-ATPase (J. Findlay and M. Harrison)
Acetylcholine receptors, between closed and open (A. Auerbach)
Functional genomics of ionotropic acetylcholine receptors in Caenorhabditis elegans and Drosophilia melanogaster (D. Satelle et al.)
Final General Discussion
Index of Contributors
Subject Index