Part I. Assessing IDPs in the Living Cell

1. Determination of IUP Based on Susceptibility for Degradation by Default

Peter Tsvetkov and Yosef Shaul

2. In-cell NMR of Intrinsically Disordered Proteins. Prokaryotic Cells

Yutaka Ito, Tsutomu Mikawa and Brian O. Smith

3. In-cell NMR in Xenopus laevis Oocytes

Rossukon Thongwichian and Philipp Selenko

4. In-cell NMR in Mammalian Cells: Part 1

Beata Bekei, Honor May Rose, Michaela Herzig, Alexander Dose, Dirk Schwarzer, and Philipp Selenko

5. In-cell NMR in Mammalian Cells: Part 2

Beata Bekei, Honor May Rose, Michaela Herzig and Philipp Selenko

6. In-cell NMR in Mammalian Cells: Part 3

Beata Bekei, Honor May Rose, Michaela Herzig, Heike Stephanowitz, Eberhard Krause, and Philipp Selenko

7. Fourier Transform Infrared Microspectroscopy of Complex Biological Systems: from Intact Cells to Whole Organisms

Diletta Ami, Antonino Natalello, and Silvia Maria Doglia

8. Studying IDP Stability and Dynamics by Fast Relaxation Imaging in Living Cells

Apratim Dhar, Maxim Prigozhin, Hannah Gelman, and Martin Gruebele

Part II. NMR-Based Techniques

9. Measurement and Analysis of NMR Residual Dipolar Couplings for the Study of Intrinsically Disordered Proteins

Loic Salmon, Malene Ringkjøbing Jensen, Pau Bernado, Martin Blackledge

^{10. Distance Information for Disordered Proteins from NMR and ESR Measurements using Paramagnetic Spin Labels}

^{David Eliezer}

^{11. Using Chemical Shifts to Assess Transient Secondary Structure and Generate Ensemble Structures of Intrinsically Disordered Proteins}

^{Stepan Kashtanov, Wade Borcherds, Hongwei Wu, Gary W. Daughdrill, F. Marty Ytreberg}

^{12. Magic Angle Spinning Solid State NMR Experiments}

^{for Structural Characterization of Proteins}

^{Lichi Shi and Vladimir Ladizhansky}

13. Wide-line NMR and Protein Hydration

Tompa K. Bokor M. Tompa P.

14. 5-Fluorotryptophan as a Dual NMR and Fluorescent Probe of a-Synuclein

Candace M. Pfefferkorn and Jennifer C. Lee

15. Aplpha Proton Detection Based on Backbone Assignment of Intrinsically Disordered Proteins

Part III. Vibrational Spectroscopy

16. Fourier Transform Infrared Spectroscopy of Intrinsically Disordered Proteins: Measurement Procedures and Data Analyses

Antonino Natalello, Diletta Ami, and Silvia Maria Doglia

17. Monitoring Stuctural Transitions in IDPs by Vibrational Spectroscopy of Cyanlated Cysteine

Hailiu Yang, Johnny Habchi, Sonia Longhi, Casey H. Londergan

18. Structure Analysis of Unfolded Peptides by Vibrational Circular Dichroism Spectroscopy

Reinhard Schweitzer-Stenner, Jonathan B. Soffer and Daniel Verbaro

19. Structural Analysis of Unfolded Peptides by Raman Spectroscopy

Reinhard Schweitzer-Stenner, Jonathan B. Soffer, Siobhan Toal and Daniel Verbaro

20. Isotope-Edited Infrared Spectroscopy

Ginka S. Buchner and Jan Kubelka

Part IV. Other Spectroscopic Techniques

21. Monitoring Structural Transitions in IDPs by site-directed Spinlabeling EPR Spectroscopy

Johnny Habchi, Marlène Martinho, Antoine Gruet, Bruno Guigliarelli, Sonia Longhi and Valérie Belle

22. Circular Dichroism Techniques for the Analysis of Intrinsically

Disordered Proteins and Domains

Lucía B. Chemes, Leonardo G. Alonso, María G. Noval and Gonzalo de Prat-Gay

23. Deconstructing Time-resolved Optical Rotatory Dispersion Kinetic Measurements of Cytochrome c Folding: From Molten Globule to the Native State

Eefei Chen and David S. Kliger

24. The use of UV-VIS Absorption Spectroscopy for Analysis of Natively Disordered Proteins

Eugene A. Permyakov

25. Intrinsic Fluorescence of Intrins