Gramicidin and Related Ion Channel-Forming Peptides
This book includes contributions from virtually all the major scientists studying gramicidin channels and is the only compilation of work in this field. It discusses crystallographic, spectroscopic, electrophysiological and computational studies, especially in the light of the recent availability of high-resolution structural data, and it compares these with insights derived from larger systems. As well as drawing together much new and exciting work in this field, it provides pointers to promising new research directions.
Correlations of Structure, Dynamics and Function in the Gramicidin Channel by Solid-State NMR Spectroscopy (T. Cross, et al.).
X-ray Crystallographic Structures of Gramicidin and Their Relation to the Streptomyces lividans Potassium Channel Structure (B. Wallace).
Design and Characterization of Gramicidin Channels with Side Chain or Backbone Mutations (R. Koeppe, et al.).
Engineering Charge Selectivity in Alamethicin Channels (G. Woolley, et al.).
Lorentzian Noise in Single Gramicidin A Channel Formamidinium Currents (T. Fairbanks, et al.).
Can We Use Rate Constants and State Models to Describe Ion Transport Through Gramicidin Channels? (S. Hladky).
The Binding Site of Sodium in the Gramicidin A Channel (B. Roux & T. Woolf).
The Mechanism of Channel Formation by Alamethicin as Viewed by Molecular Dynamics Simulations (M. Sansom, et al.).
Ionic Interactions in Multiply Occupied Channels (V. Dorman, et al.).
Peptide Influences on Lipids (J. Killian, et al.).
Lipid Interactions and Mechanisms of Antimicrobial Peptides (H. Huang).
Folding Patterns of Membrane Proteins: Diversity and the Limitations of Their Prediction (J. Rosenbusch).
Molecular Basis of the Charge Selectivity of Nicotinic Acetylcholine Receptor and Related Ligand-Gated Ion Channels (P.-J. Corringer, et al.).
The Gramicidin-Based Biosensor: A Functioning Nano-Machine (B. Cornell, et al.).
Final General Discussion: Protons.
Summary: What We Have Learned About Gramicidin and Other Ion Channels.