Intrinsically Disordered Protein Analysis: Volume 2, Methods and Experimental Tools (Hardcover, 2012)

Part I. Single Molecule Techniques 1. Immobilization of Proteins for Single Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics Ucheor B. Choi, Keith R. Weninger, and Mark E. Bowen 2. Application of Confocal Single Molecule FRET to Intrinsically Disordered Proteins Benjamin Schuler, Sonja Muller-Spath, Andrea Sorranno, Daniel Nettles 3. Single-Molecule Force Spectroscopy of Chimeric Polyprotein Constructs Containing Intrinsically Disordered Domains Marco Brucale, Isabella Tessari, Luigi Bubacco, Bruno Samori 4. Visualization of Mobility by Atomic Force Microscopy Toshio Ando and Noriyuki Kodera 5. Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered Proteins Javier Oroz, Ruben Hervas, Alejandro Valbuena & Mariano Carrion-Vazquez Part II. Methods to Assess Protein Size and Shape 6. Sedimentation Velocity Analytical Ultracentrifugation for Intrinsically Disordered Proteins Andres G. Salvay, Guillaume Communie, and Christine Ebel 7. Analysis of Intrinsically Disordered Proteins by Small-Angle X-ray Scattering Pau Bernado and Dmitri I. Svergun 8. Small Angle Neutron Scattering (SANS) for the Structural Study of Intrinsically Disordered Proteins in Solution: a Practical Guide Frank Gabel 9. Dynamic and Static Light Scattering of Intrinsically Disordered Proteins Klaus Gast and Christian Fiedler 10. Estimation of Intrinsically Disordered Protein Shape and Time-averaged Apparent Hydration in Native Conditions by a Combination of Hydrodynamic Methods Johanna C. Karst, Ana Cristina Sotomayor-Perez, Daniel Ladant and Alexandre Chenal 11. Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins Vladimir N. Uversky Part III. Methods to Analyze Conformational Behavior 12. Denaturant-induced Conformational Transitions in Intrinsically Disordered Proteins Paolo Neyroz, Stefano Ciurli, and Vladimir N. Uversky 13. Identification of Intrinsically Disordered Proteins by a Special 2D Electrophoresis Agnes Tantos, Peter Tompa 14. pH-induced Changes in Intrinsically-disordered Proteins Matthew D. Smith and Masoud Jelokhani-Niaraki 15. Temperature Induced Transitions in Disordered Proteins Probed by NMR Spectroscopy Magnus Kjaergaard, Flemming M. Poulsen and Birthe B. Kragelund 16. Analyzing Temperature Induced Transitions in Disordered Proteins by NMR Spectroscopy and Secondary Chemical Shift Analyses Magnus Kjaergaard, Flemming M. Poulsen & Birthe B. Kragelund 17. Osmolyte-, Binding-, and Temperature-Induced Transitions of Intrinsically Disordered Proteins Allan Chris M. Ferreon and Ashok A. Deniz 18. Laser Temperature-jump Spectroscopy of Intrinsically Disordered Proteins Stephen J. Hagen 19. Differential Scanning Microcalorimetry of Intrinsically Disordered Proteins Sergei E. Permyakov 20. Identifying Disordered Regions in Proteins by Limited Proteolysis Angelo Fontana, Patrizia Polverino de Laureto, Barbara Spolaore and Erica Frare 21. The Effect of Counter Ions on the Conformation of Intrinsically Disordered Proteins Studied by Size-exclusion Chromatography Magdalena Wojtas, Tomasz M. Kaplon, Piotr Dobryszycki, Andrzej Ozyhar 22. Mean Net Charge of Intrinsically Disordered Proteins: Experimental Determination of Protein Valence by Electrophoretic Mobility Measurements Ana Cristina Sotomayor-Perez, Johanna C. Karst, Daniel Ladant and Alexandre Chenal 23. Protein Characterization by Partitioning in Aqueous Two-Phase Systems Larissa Mikheeva, Pedro Madeira, and Boris Zaslavsky Part IV. Mass-Spectrometry 24. Detection and Characterization of Large-scale Protein Conformational Transitions in Solution using Charge-state Distribution Analysis in ESI-MS Rinat R. Abzalimov, Agya K. Frimpong and Igor A. Kaltashov 25. Localizing Flexible Regions in Proteins using Hydrogen Deuterium Exchange Mass Sp