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Bücher | August 2005 | Protein-Lipid Interactions
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Tamm, Lukas K. (Hrsg.)
Protein-Lipid Interactions
From Membrane Domains to Cellular Networks

1. Auflage - August 2005
179,- Euro
2005. XXVI, 444 Seiten, Hardcover
82 Abb. (24 Farbabb.), 3 Tab. 
- Handbuch/Nachschlagewerk -
ISBN-10: 3-527-31151-3
ISBN-13: 978-3-527-31151-4 - Wiley-VCH, Weinheim

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Kurzbeschreibung
This first comprehensive handbook examines biophysical principles of membrane thermodynamics and structure, and goes on to discuss biochemical and cell biology processes, including mechanisms of membrane fusion and fission, pore-forming toxins and lipid rafts.

Aus dem Inhalt
HOW LIPIDS SHAPE PROTEINS
Lipid Bilayers, Translocons, and the Shaping of Polypeptide Structure
Folding and Stability of Monomeric beta-Barrel Membrane Proteins
Principles, Kinetics and Stability of Bacteriorhodopsin Folding
Post-Integration Misassembly of Membrane Proteins and Disease

HOW PROTEINS SHAPE LIPIDS
A Census of Ordered Lipids and Detergents in X-ray Crystal Structures of Integral Membrane Proteins
Lipid and Detergent Interactions with Membrane Proteins Derived from Solution NMR

MEMBRANE PENETRATION BY TOXINS
Lipid Interactions of alpha-Helical Protein Toxins
Membrane Recognition and Pore Formation by Bacterial Pore-forming Toxins
Mechanism of Membrane Permeation and Pore Formation by Antimicrobial Peptides

MECHANISMS OF MEMBRANE FUSION
Cell Fusion in Development and Disease
Molecular Mechanisms of Intracellular Membrane Fusion
Interplay of Proteins and Lipids in Virus Entry by Membrane Fusion

CHOLESTEROL, LIPID RAFTS, AND PROTEIN SORTING
Protein-Lipid Interactions in the Formation of Raft Microdomains
Protein and Lipid Partitioning in Locally Heterogeneous Model Membranes

TARGETING OF EXTRINSIC MEMBRANE PROTEIN MODULES TO MEMBRANES AND SIGNAL TRANSDUCTION
In vitro and Cellular Membrane Binding Mechanisms of Membrane Targeting Domains
Structure and Interactions of C2 Domains at Membrane Surfaces
Structural Mechanisms of Allosteric Regulation by Membrane-binding domains


 
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