Book contents
- Frontmatter
- Contents
- Preface
- 1 Introduction
- 2 The Diversity of Membrane Lipids
- 3 Tools for Studying Membrane Components: Detergents and Model Systems
- 4 Proteins in or at the Bilayer
- 5 Bundles and Barrels
- 6 Functions and Families
- 7 Protein Folding and Biogenesis
- 8 Diffraction and Simulation
- 9 Membrane Enzymes and Transducers
- 10 Transporters and Channels
- 11 Membrane Protein Assemblies
- 12 Themes and Future Directions
- Appendix I Abbreviations
- Appendix II Single-Letter Codes for Amino Acids
- Index
- References
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4 - Proteins in or at the Bilayer
Book contents
- Frontmatter
- Contents
- Preface
- 1 Introduction
- 2 The Diversity of Membrane Lipids
- 3 Tools for Studying Membrane Components: Detergents and Model Systems
- 4 Proteins in or at the Bilayer
- 5 Bundles and Barrels
- 6 Functions and Families
- 7 Protein Folding and Biogenesis
- 8 Diffraction and Simulation
- 9 Membrane Enzymes and Transducers
- 10 Transporters and Channels
- 11 Membrane Protein Assemblies
- 12 Themes and Future Directions
- Appendix I Abbreviations
- Appendix II Single-Letter Codes for Amino Acids
- Index
- References
Summary
The chemical and physical properties of the lipids described in Chapter 2 make it clear that the lipid bilayer provides a special milieu for proteins. Its constraints affect the structure, function, and regulation of proteins that dock on it or assemble in it to perform jobs such as energy transduction, nutrient transport, and signaling. The variety among proteins that interact in some way with the membrane is quite astonishing and provides fascinating examples of how these proteins are structured to work in their environment.
This chapter first defines the classes of proteins that are found in or at the bilayer. It describes many examples of peripheral proteins, as well as some lipid-anchored proteins, before looking at what modulates the interactions of these proteins with membrane lipids. Next it focuses on molecules that insert into the membrane, including examples of toxins, colicins, and ion-carrying peptides. Then a look at the special qualities of the nonpolar milieu of the membrane explains many characteristics of integral membrane proteins. The chapter ends with studies of protein–lipid interactions in membranes.
CLASSES OF PROTEINS THAT INTERACT WITH THE MEMBRANE
A typical biomembrane contains many species of proteins, some embedded in the lipid bilayer and others on its surface. The Fluid Mosaic Model described in Chapter 1 distinguished between extrinsic and intrinsic membrane proteins by how easily they could be isolated from the membrane: extrinsic (peripheral) proteins can be removed by washes of the membrane, while the extraction of intrinsic (integral) proteins requires disruption of the membrane.
- Type
- Chapter
- Information
- Membrane Structural BiologyWith Biochemical and Biophysical Foundations, pp. 68 - 101Publisher: Cambridge University PressPrint publication year: 2008
References
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, and , The protein–lipid interface: perspectives from magnetic resonance and crystal structures. Biochim Biophys Acta. 2004, 1666:118–141.CrossRefGoogle ScholarPubMed
, , and , Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol. 2005, 6:449–461.CrossRefGoogle ScholarPubMed
Heimburg, T., and D. Marsh, Thermodynamics of the interaction of proteins with lipid membranes, in and (eds.), Biological Membranes. Cambridge, Mass.: Birkhauser, 1996, pp. 405–462.CrossRefGoogle Scholar
, and , Signaling and subcellular targeting by membrane-binding domains. Annu Rev Biophys Biomol Struct. 2000, 29:49–70.CrossRefGoogle ScholarPubMed
, and , Amphoteric proteins: regulation by reversible membrane interactions. Biochim Biophys Acta. 1999, 16:217–235.Google Scholar
, and , Sorting GPI-anchored proteins. Nat Rev Mol Cell Biol. 2004, 5:110–119.CrossRefGoogle ScholarPubMed
, and , The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem Sci. 1995, 20:272–276.CrossRefGoogle ScholarPubMed
Seaton, B. A., and M. F. Roberts, Peripheral membrane proteins, in and (eds.), Biological Membranes. Cambridge, Mass.: Birkhauser, 1996, pp. 355–403.CrossRefGoogle Scholar
, and , Penetration of protein toxins into cells. Curr Opin Cell Biol. 2000, 12:407–413.CrossRefGoogle ScholarPubMed
, α-Hemolysin from Staphylococcus aureus: an archetype of β-barrel, channel-forming toxins. J Struct Biol. 1998, 121:110–122.CrossRefGoogle ScholarPubMed
, and , Colicin crystal structures: pathways and mechanisms for colicin insertion into membranes. Biochim Biophys Acta. 2002, 1565:333–346.CrossRefGoogle ScholarPubMed
, and , Insertion intermediates of pore-forming colicins in membrane two-dimensional space. Biochimie. 2002, 84:465–475.CrossRefGoogle ScholarPubMed
, et al., On the role of lipid in colicin pore formation. Biochim Biophys Acta. 2004, 1666:239–249.CrossRefGoogle ScholarPubMed
, and , Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr Opin Struct Biol. 2003, 13:412–417.CrossRefGoogle ScholarPubMed
, and , Helical membrane protein folding, stability and evolution. Annu Rev Biochem. 2000, 69:881–922.CrossRefGoogle ScholarPubMed
, and , Transmembrane helices before, during and after insertion. Curr Opin Struct Biol. 2005, 15:378–386.CrossRefGoogle ScholarPubMed
, et al., How membranes shape protein structure. J Biol Chem. 2001, 276:32395–32398.CrossRefGoogle ScholarPubMed
, How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta. 2004, 1666:62–87.Google ScholarPubMed
, Lipid–protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta. 2003, 1612:1–40.CrossRefGoogle ScholarPubMed
, and , Structure, dynamics and composition of the lipid–protein interface. Perspectives from spin-labelling. Biochim Biophys Acta. 1998, 1376:267–296.CrossRefGoogle ScholarPubMed
, and , The protein–lipid interface: perspectives from magnetic resonance and crystal structures. Biochim Biophys Acta. 2004, 1666:118–141.CrossRefGoogle ScholarPubMed