Chapter 2. Folding and Stability of Monomeric β-Barrel Membrane Proteins

  1. Prof. Dr. Lukas K. Tamm
  1. Priv.-Doz. Jörg H. Kleinschmidt

Published Online: 29 MAR 2006

DOI: 10.1002/3527606769.ch2

Protein-Lipid Interactions: From Membrane Domains to Cellular Networks

Protein-Lipid Interactions: From Membrane Domains to Cellular Networks

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

  1. Professor of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, VA 22908-0736, USA

Author Information

  1. Department of Biology (M 694), University of Konstanz, 78457 Konstanz, Germany

Publication History

  1. Published Online: 29 MAR 2006
  2. Published Print: 5 AUG 2005

ISBN Information

Print ISBN: 9783527311514

Online ISBN: 9783527606764

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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