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Intrinsically Disordered Protein Analysis, Volume 1: Methods and Experimental Tools

Handbook / Manual

Series: Methods in Molecular Biology Volume: 895

By: Vladimir N Uversky (Editor), A Keith Dunker (Editor)

525 pages, 76 colour & 62 b/w illustrations, 5 tables

Humana Press

Hardback | Jul 2012 | #205755 | ISBN-13: 9781617799266
Availability: Usually dispatched within 1-2 weeks Details
NHBS Price: £108.00 $132/€121 approx

About this book

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, Volume 1: 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 1 includes sections on assessing IDPs in the living cell,NMR based techniques, vibrational spectroscopy, and other spectroscopic techniques. Written in the highly successful Methods in Molecular Biology 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, Volume 1: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules.


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 Ringkjobing 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, Marlene Martinho, Antoine Gruet, Bruno Guigliarelli, Sonia Longhi and Valerie Belle
22. Circular Dichroism Techniques for the Analysis of Intrinsically Disordered Proteins and Domains Lucia B. Chemes, Leonardo G. Alonso, Maria 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 Intrinsically Disordered Proteins Paolo Neyroz and Stefano Ciurli
26. Binding Stoichiometry and Affinity of Fluorescent Dyes to Proteins in Different Structural States Anna I. Sulatskaya, Olga I. Povarova, Irina M. Kuznetsova, Vladimir Uversky and Konstantin K. Turoverov
27. Fluoresnece Lifetime Measurements of Intrinsically Unstructured Proteins-Applications to Alpha-Synuclein Sarah Schreurs, Malgorzata Kluba, Jessika Meuvis, and Yves Engelborghs
28. Ensemble FRET Methods in Studies of Intrinsically Disordered Proteins Elisha Haas
29. Fluorensce Correlation Spectroscopy to Determine the Diffusion Coefficient of the and Follow Early Formation Sangeeta Nath, Manli Deng, and Yves Engelborghs

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