Dunker / Uversky | Intrinsically Disordered Protein Analysis | Buch | 978-1-61779-926-6 | sack.de

Buch, Englisch, Band 895, 511 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 1179 g

Reihe: Methods in Molecular Biology

Dunker / Uversky

Intrinsically Disordered Protein Analysis

Volume 1, Methods and Experimental Tools
2012
ISBN: 978-1-61779-926-6
Verlag: Humana Press

Volume 1, Methods and Experimental Tools

Buch, Englisch, Band 895, 511 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 1179 g

Reihe: Methods in Molecular Biology

ISBN: 978-1-61779-926-6
Verlag: Humana Press


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 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: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules.

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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 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, Jessi



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