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Table of Contents:
Preface
Section 1. - NMR and EPR Spectroscopy
Chapter 1.1 - Analyzing Protein Folding by NMR; pp. 3-32
(Balbach J.)
Chapter 1.2 - EPR Methods for Evaluating Copper Binding Sites in Prion and other Partially Structured Proteins; pp. 33-45
(Millhauser G.L.)
Chapter 1.3 - Variable Velocity Liquid Flow EPR and Submillisecond Protein Folding; pp. 47-71
(Grigoryants V.M., Scholes C.P.)
Chapter 1.4 - EPR/ESR/EMR Methods for Studying Calcium Binding Proteins; pp. 73-92
(Berliner L.J.)
Section 2. - Mass-Spectrometry
Chapter 2.1 - Stopped-flow Electrospray Ionization Mass Spectrometry; pp. 95-119
(Konermann L., Wilson D.J., Simmons D.A.)
Chapter 2.2 - Modern Mass Spectrometry and Proteomic Methods Applied to Biomarker Identification and Drug Target Discovery; pp. 121-174
(Durr E.)
Chapter 2.3 - Analysis of Partially Folded Proteins by Electron Ionization Mass Spectrometry; pp. 175-196
(Kaltashov I.)
Section 3. - Protein Imaging
Chapter 3.1 - Protein Imaging: Scanning Probe Microscopy;
pp. 199-218
(Yaminsky I.)
Chapter 3.2 - Cryo-electron Microscopy as a Tool to Study Molecular Machines; pp. 219-232
(Frank J.)
Section 4. - Miscellaneous
Chapter 4.1 - Time-resolved Optical Rotatory Dispersion Studies of Azobenzene Cross-Linked Peptides; pp. 235-255
(Chen E., Woolley G.A., Kliger D.S.)
Chapter 4.2 - Phase Diagram Method for Analysis of Protein Folding; pp. 257-318
(Turoverov K.K., Kuznetsova I.A., Uversky V.N.)
Chapter 4.3 - The use of Protein Engineering Methods for Studies of Calcium Binding Proteins; pp. 319-350
(Permyakov E.A.)
Chapter 4.4 - Analysis of Membrane-bound Protein Association using Fluorescence Spectroscopy; pp. 351-361
(Scarlata S.)
Chapter 4.5 - The Role of Aromatic Interactions in Folding, Stability and Molecular Recognition of Proteins and Polypeptides; pp. 363-374
(Gilead S., Gazit E.)
Index |
