Membrane Proteins 1st Edition by Douglas Rees ISBN 0120342634 978-0120342631

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ISBN 10:  0120342634 

ISBN 13: 978-0120342631

Author:  Douglas C. Rees

The book delves into the biophysical, biochemical, and structural properties of membrane proteins, examining how they interact with their environment and contribute to cellular functions. The contributions come from leading experts in the field and are organized to provide an in-depth exploration of the latest research and methodologies used to study these complex proteins.

Key Features:
Structural Biology Focus: The book covers the advances in crystallography, NMR, and other techniques used to determine the 3D structures of membrane proteins, emphasizing how structure dictates function.

Membrane Protein Classification: It discusses the diverse types of membrane proteins, such as transporters, receptors, and enzymes, and their roles in various cellular and physiological processes.

Mechanisms of Action: The text explores the mechanisms by which membrane proteins function, including how they facilitate transport across lipid bilayers, their involvement in cell signaling, and their role in disease mechanisms.

Methodologies and Techniques: The book also includes chapters on the experimental methods used to study membrane proteins, such as electrophysiology, spectroscopy, and cryo-electron microscopy.

Clinical Relevance: There is a focus on the medical implications of membrane proteins, particularly in relation to drug design, pharmacology, and understanding diseases such as cystic fibrosis and cancer.

Table of contents: 

Membrane Protein Assembly in Vivo

GUNNAR VON HEIJNE

I. Introduction

II. Overview of Membrane Protein Assembly Pathways in Prokaryotic and Eukaryotic Cells

III. Membrane Protein Assembly in the ER

IV. Membrane Protein Assembly in Escherichia coli

V. Membrane Protein Assembly in Mitochondria

VI. Membrane Protein Assembly in Chloroplasts

VII. Membrane Protein Assembly in Peroxisomes

VIII. Conclusions

References.

Construction of Helix-Bundle Membrane Proteins

Aaron K. Chamberlain, Salem Fahm, Sarah Yohannan, and James U. Bowie.

I. Introduction

II. Transmembrane Helix Structure

III. Thermodynamic Studies

IV. The Contribution of Loops versus Transmembrane Helices

V

V. Forces That Stabilize Transmembrane Helix Interactions.

VI. Conclusions

References.

Transmembrane B-Barrel Proteins

GEORG E. SCHULZ

I. Introduction

II. Structures

III. Construction Principles

IV. Functions

V. Folding and Stability

VI. Channel Engineering.

VII. Conclusions References.

Length, Time, and Energy Scales of Photosystems

CHRISTOPHER C. MOSER, CHRISTOPHER C. PAGE, RICHARD J. COGDELE

JAMES BARBER, COLIN A. WRAIGHT, AND P. LESLIE DUTTON

I. Introduction

II. Overview of Length Scales in Bioenergetic Membranes

III. Managing Lengths in Natural Redox Protein Design

IV. Managing Length and Size in Natural Light-Harvesting Design

V. Managing Distance in Electron Transfer

VI. Managing Proton Reactions in Photosynthesis

VII. Managing Diffusion in Photosynthesis

VIII. Summary

References.

Structural Clues to the Mechanism of lon Pumping in Bacteriorhodo

HARTMUT LUECKE AND JANOS K. LANYI

I. Introduction

II. The Ground, or Resting, State

III. Early Photocycle Intermediates (Kand L.).

The Glycerol Facilitator GlpF, Its Aquaporin Family of Channels, and Their Selectivity
By: Robert M. Stroud, Peter Nollert, and Larry Miercke

I. An Ancient and Long Recognized Channel
Discovery of the GlpF channel and its crucial role in transporting glycerol across the cell membrane.

II. Three-Dimensional Structure of GlpF with Glycerol in Transit
Description of the three-dimensional structure of GlpF as glycerol moves through the channel.

III. The Basis for Selectivity through the Channel
Explanation of the selectivity mechanism of GlpF, how it differentiates glycerol from other molecules.

IV. Roles of Conserved Residues: Functional and Structural
The importance of conserved residues in the structure and function of GlpF.

V. Stereoselective Preferences of GlpF among Linear Alditols
GlpF has a stereoselective preference for glycerol and other linear alditols.

VI. Simulations and Rates of Glycerol Passing through the Channel
Simulations and evaluation of the rate at which glycerol passes through the GlpF channel.

VII. Simulation and Rates of Water Passage through the GlpF (an AQP) Channel
Assessment of the speed and mechanism of water passing through the GlpF channel (a member of the AQP family).

VIII. Insulation against Proton Conduction in AQPs
Analysis of insulation against proton conduction in AQPs.

IX. Quaternary Structure of GlpF (and AQPs)
The quaternary structure of GlpF and other AQPs, and how they are organized.

X. The Ion Channel in AQP6; a Possible Pore on the Fourfold Axis of AQPs?
AQP6 and the hypothesis of an ion pore on the fourfold axis of AQPs.

XI. GlpF Channel Selectivity for Antimonite
The selectivity of the GlpF channel for antimonite.

XII. Selectivity against Passing Ions or an Electrochemical Gradient
Analysis of the rejection of ion passage or electrochemical gradient through the GlpF channel.

XIII. The Various Contributions to Rejection of Proton Conductance
The factors contributing to the rejection of proton conduction in AQPs.

XIV. Selectivity for Glycerol versus Water
The mechanism by which GlpF distinguishes between glycerol and water in its transport.

XV. Regulated Ion Channels Formed by Members of the AQP Family
Ion channels regulated by members of the AQP family.

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