Description
Book SynopsisThe Amphipathic Helix is a comprehensive volume discussing amphipathic helices in systems as diverse as serum lipoproteins, lung surfactant, cytotoxic peptides, ion channels, mitochondrial targeting, peptide hormones, G proteins, T-cell recognition, DNA binding proteins, and antifreeze proteins. The book also includes general introductory material that defines amphipathic helices, discusses methods to identify amphipathic helical segments from the amino acid sequence of a protein, illustrates how amphipathic helices can be used in the de novo design of peptide and protein structures, and describes how these helices stabilize protein structures. There is also a section on techniques to determine helix orientation in a membrane environment using polarized attenuated total reflection infrared spectroscopy or solid state NMR spectroscopy. Recent developments on all these topics have been discussed by leading experts in this reference for researchers and students in biochemistry, biophysics
Table of ContentsIntroduction and Overview (R.M. Epand). Design of Amphipathic Helices: Computational Techniques to Predict Amphipathic Helical Segments (I.E. Auger). Amphipathic Helices in Designed Peptide Structures (J.M. Stewart). The Role of Amphipathic Helices in Stabilizing Peptide and Protein Structure (C.T. Mant, N.E. Zhou, and R.S. Hodges). Experimental Methods for Studying Amphipathic Helices in Membranes: Polarized Attenuated Total Reflection Infrared Spectroscopy as a Tool to Investigate the Structure and Orientation of Amphipathic Peptides in a Lipid Bilayer (E. Goormaghtigh, V. Cabiaux, and J.-M. Ruysschaert). NMR Spectroscopy of Amphipathic Helical Peptides in Membrane Environments (S.J. Opella, J. Gesell, and B. Bechinger). Biological Roles for the Interactions of Amphipathic Helices with Lipids: An Atlas of the Amphipathic Helical Domains of the Human Exchangeable Plasma Apolipoproteins (G.M. Anantharamaiah, M.K. Jones, and J.P. Segrest). Amphipathic Helical Segments in Lung Surfactant Proteins (A.J. Waring, L.M. Gordon, H.W. Taeusch, and R. Bruni). The Amphipathic Helix in Cytotoxic Peptides (I. Cornut, E. Thiaudière, and J. Dufourcq). Amphipathic Helices and Ion Channels (J. Tomich). Other Biological Roles for Amphipathic Helices in Membrane-Related Phenomenon: The Amphipathic Helix in Mitochondrial Targeting Sequences (D. Roise). Amphiphilic Helices in Neuropeptides (J.W. Taylor). Activation of G Proteins by Membrane Receptors and Peptides. Putative Role for Amphipathic Helices (M. Mousli and Y. Landry). The Amphipathic Helix as a Structural Feature Involved in T-Cell Recognition (J.L. Cornette, H. Margalit, C. DeLisi, and J.A. Berzofsky). Other Biological Roles of Amphipathic Helices: Amphipathic Helices in Proteins that Bind to DNA: The bZIP and bHLH-Zip DNA Binding Motifs (C.R. Vinson). Protein-Ice Interactions: Antifreeze Proteins (D.S.C. Yang).
