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Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins. Structural biologists now recognize that the functional diversity provided by disordered regions complements the functional repertoire of ordered protein regions. In Intrinsically Disordered Protein Analysis: Methods and Experimental Tools, expert researchers explore the high abundance of IDPs in various organisms, their unique structural features, numerous functions, and crucial associations with different diseases. Volume 2 includes sections on single molecule techniques, methods to assess protein size and shape, analyzing conformational behavior, mass-spectrometry, expression and purification of IDP's. Written in the highly successful Methods in Molecular Biology(TM) series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Intrinsically Disordered Protein Analysis: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules.
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Table of Contents

Part I. Single Molecule Techniques1. Immobilization of Proteins for Single Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and DynamicsUcheor B. Choi, Keith R. Weninger, and Mark E. Bowen2. Application of Confocal Single Molecule FRET to Intrinsically Disordered ProteinsBenjamin Schuler, Sonja Muller-Spath, Andrea Sorranno, Daniel Nettles3. Single-Molecule Force Spectroscopy of Chimeric Polyprotein Constructs Containing Intrinsically Disordered DomainsMarco Brucale, Isabella Tessari, Luigi Bubacco, Bruno Samori4. Visualization of Mobility by Atomic Force MicroscopyToshio Ando and Noriyuki Kodera5. Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered ProteinsJavier Oroz, Ruben Hervas, Alejandro Valbuena & Mariano Carrion-VazquezPart II. Methods to Assess Protein Size and Shape6. Sedimentation Velocity Analytical Ultracentrifugation for Intrinsically Disordered ProteinsAndres G. Salvay, Guillaume Communie, and Christine Ebel7. Analysis of Intrinsically Disordered Proteins by Small-Angle X-ray ScatteringPau Bernado and Dmitri I. Svergun 8. Small Angle Neutron Scattering (SANS) for the Structural Study of Intrinsically Disordered Proteins in Solution: a Practical GuideFrank Gabel9. Dynamic and Static Light Scattering of Intrinsically Disordered ProteinsKlaus Gast and Christian Fiedler10. Estimation of Intrinsically Disordered Protein Shape and Time-averaged Apparent Hydration in Native Conditions by a Combination of Hydrodynamic MethodsJohanna C. Karst, Ana Cristina Sotomayor-Perez, Daniel Ladant and Alexandre Chenal11. Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins Vladimir N. UverskyPart III. Methods to Analyze Conformational Behavior12. Denaturant-induced Conformational Transitions in Intrinsically Disordered ProteinsPaolo Neyroz, Stefano Ciurli, and Vladimir N. Uversky13. Identification of Intrinsically Disordered Proteins by a Special 2D ElectrophoresisAgnes Tantos, Peter Tompa14. pH-induced Changes in Intrinsically-disordered ProteinsMatthew D. Smith and Masoud Jelokhani-Niaraki15. Temperature Induced Transitions in Disordered Proteins Probed by NMR SpectroscopyMagnus Kjaergaard, Flemming M. Poulsen and Birthe B. Kragelund16. Analyzing Temperature Induced Transitions in Disordered Proteins by NMR Spectroscopy and Secondary Chemical Shift AnalysesMagnus Kjaergaard, Flemming M. Poulsen & Birthe B. Kragelund17. Osmolyte-, Binding-, and Temperature-Induced Transitions of Intrinsically Disordered ProteinsAllan Chris M. Ferreon and Ashok A. Deniz 18. Laser Temperature-jump Spectroscopy of Intrinsically Disordered ProteinsStephen J. Hagen19. Differential Scanning Microcalorimetry of Intrinsically Disordered Proteins Sergei E. Permyakov20. Identifying Disordered Regions in Proteins by Limited ProteolysisAngelo Fontana, Patrizia Polverino de Laureto, Barbara Spolaore and Erica Frare21. The Effect of Counter Ions on the Conformation of Intrinsically Disordered Proteins Studied by Size-exclusion ChromatographyMagdalena Wojtas, Tomasz M. Kaplon, Piotr Dobryszycki, Andrzej Ozyhar22. Mean Net Charge of Intrinsically Disordered Proteins: Experimental Determination of Protein Valence by Electrophoretic Mobility MeasurementsAna Cristina Sotomayor-Perez, Johanna C. Karst, Daniel Ladant and Alexandre Chenal23. Protein Characterization by Partitioning in Aqueous Two-Phase SystemsLarissa Mikheeva, Pedro Madeira, and Boris Zaslavsky Part IV. Mass-Spectrometry24. 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. Kaltashov25. Localizing Flexible Regions in Proteins using Hydrogen Deuterium Exchange Mass SpectrometryCedric E. Bobst and Igor A. Kaltashov26. Mass-spectrometry Tools for Analysis of Intermolecular Interactions Jared R. Auclair, Mohan Somasundaran, Karin M. Green, James E. Evans, Celia A. Schiffer, Dagmar Ringe, Gregory A. Petsko, and Jeffrey N. Agar27. Characterization of Oligomerization- Aggregation Products of Neurodegenerative Target Proteins by Ion Mobility Mass SpectrometryCamelia Vlad, Marius Ionut Iurascu, Stefan Slamnoiu, Bastian Hengerer, and Michael PrzybylskiPart V. Expression and Purification of IDP's 28. Identifying Solubility-promoting Buffers for Intrinsically Disordered Proteins Prior to PurificationKelly A. Churion and Sarah E. Bondos29. Proteomic Methods for the Identification of Intrinsically Disordered Proteins Agnes Tantos, Peter Tompa30. Selective Isotope Labeling of Recombinant Proteins in E. coliKit I. Tong, Masayuki Yamamoto, and Toshiyuki Tanaka

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