Chapter 2. Folding and Stability of Monomeric β-Barrel Membrane Proteins
- Prof. Dr. Lukas K. Tamm
Published Online: 29 MAR 2006
DOI: 10.1002/3527606769.ch2
Copyright © 2005 Wiley-VCH Verlag GmbH & Co. KGaA
Book Title

Protein-Lipid Interactions: From Membrane Domains to Cellular Networks
Additional Information
How to Cite
Kleinschmidt, J. H. (2006) Folding and Stability of Monomeric β-Barrel Membrane Proteins, in Protein-Lipid Interactions: From Membrane Domains to Cellular Networks (ed L. K. Tamm), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG. doi: 10.1002/3527606769.ch2
Editor Information
Professor of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, VA 22908-0736, USA
Publication History
- Published Online: 29 MAR 2006
- Published Print: 5 AUG 2005
ISBN Information
Print ISBN: 9783527311514
Online ISBN: 9783527606764
- Summary
- Chapter
Keywords:
- folding and stability of monomeric β-barrel membrane proteins;
- stability of β-barrel membrane proteins;
- insertion and folding of transmembrane β-barrel proteins;
- kinetics of membrane protein folding;
- orientation of β-barrel membrane proteins in lipid bilayers;
- in vivo requirements for the folding of OMPs
Summary
This chapter contains sections titled:
Introduction
Stability of β-Barrel Membrane Proteins
Thermodynamic Stability of FepA in Detergent Micelles
Thermodynamic Stability of OmpA in Phospholipids Bilayers
Thermal Stability of FhuA in Detergent Micelles
Insertion and Folding of Transmembrane β-Barrel Proteins
Insertion and Folding of β-Barrel Membrane Proteins in Micelles
Oriented Insertion and Folding into Phospholipid Bilayers
Assemblies of Amphiphiles Induce Structure Formation in β-Barrel Membrane Proteins
Electrophoresis as a Tool to Monitor Insertion and Folding of β-Barrel Membrane Proteins
pH and Lipid Headgroup Dependence of the Folding of β-Barrel Membrane Proteins
Kinetics of Membrane Protein Folding
Rate Law for β-Barrel Membrane Protein Folding and Lipid Acyl Chain Length Dependence
Synchronized Kinetics of Secondary and Tertiary Structure Formation of the β-Barrel OmpA
Interaction of OmpA with the Lipid Bilayer is Faster than the Formation of Folded OmpA
Folding Mechanism of the β-Barrel of OmpA into DOPC Bilayers
Multistep Folding Kinetics and Temperature Dependence of OmpA Folding
Characterization of Folding Intermediates by Fluorescence Quenching
The β-Barrel Domain of OmpA Folds and Inserts by a Concerted Mechanism
Protein–Lipid Interactions at the Interface of β-Barrel Membrane Proteins
Stoichiometry of the Lipid–Protein Interface
Lipid Selectivity of β-Barrel Membrane Proteins
Orientation of β-Barrel Membrane Proteins in Lipid Bilayers
Lipid Dependence of the β-Barrel Orientation Relative to the Membrane
Inclination of the β-Strands Relative to the β-Barrel Axis in Lipid Bilayers
Hydrophobic Matching of the β-Barrel and the Lipid Bilayer
In vivo Requirements for the Folding of OMPs
Amino Acid Sequence Constraints for OmpA Folding in vivo
Periplasmic Chaperones
Insertion and Folding of the β-Barrel OmpA is Assisted by Skp and LPS
Role of Omp85 in Targeting or Assembly of β-Barrel Membrane Proteins
Outlook
References
