Intrinsically disordered protein analysis. Volume 1, Methods and experimental tools / edited by Vladimir N. Uversky, A. Keith Dunker.
Material type:
TextSeries: Methods in molecular biology (Clifton, N.J.) ; v. 895.Publication details: New York : Humana Press : Springer, ©2012.Description: 1 online resource (xiv, 511 pages) : illustrations (some color)Content type: - text
- computer
- online resource
- 9781617799273
- 1617799270
- 1617799262
- 9781617799266
- Methods and experimental tools
- Proteins -- Laboratory manuals
- Proteins -- Denaturation -- Laboratory manuals
- Proteins -- Analysis -- Laboratory manuals
- Proteins -- Denaturation
- Proteins
- Protein Denaturation
- Proteins
- Proteins -- analysis
- Life Sciences
- Protein Science
- Protein Structure
- Protéines -- Manuels de laboratoire
- Protéines -- Dénaturation -- Manuels de laboratoire
- Protéines -- Analyse -- Manuels de laboratoire
- Protéines -- Dénaturation
- Protéines
- protein
- Proteins
- Proteins -- Analysis
- Proteins -- Denaturation
- Life sciences
- Biochemistry
- Protein Science
- Protein Structure
- eiwitten
- proteins
- Proteins and Enzymes
- Eiwitten en enzymen
- 572/.6 23
- QP551 .I58 2012
- QP551 .I627 2012 v.1
| Item type | Current library | Collection | Call number | Status | Date due | Barcode | Item holds | |
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eBook
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e-Library | eBook Protocols | Available |
Includes bibliographical references and index.
Online resource; title from PDF title page (Springer Protocols, viewed Oct. 18, 2012).
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.
English.
Determination of IUP based on susceptibility for degradation by default / Peter Tsvetkov, Yosef Shaul -- In-cell NMR of intrinsically disordered proteins in prokaryotic cells / Yutaka Ito, Tsutomu Mikawa, Brian O. Smith -- In-cell NMR in Xenopus laevis oocytes / Rossukon Thongwichian, Philipp Selenko -- In-cell NMR in mammalian cells : part 1 / Beata Bekei ... [et al.] -- In-cell NMR in mammalian cells : part 2 / Beata Bekei ... [et al.] -- In-cell NMR in mammalian cells : part 3 / Beata Bekei ... [et al.] -- Fourier transform infrared microspectroscopy of complex biological systems : from intact cells to whole organisms / Diletta Ami, Antonino Natalello, Silvia Maria Doglia -- Studying IDP stability and dynamics by fast relaxation imaging in Living Cells / Apratim Dhar ... [et al.] -- Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered Proteins / Loic Salmon ... [et al.] -- Distance information for disordered proteins from NMR and ESR measurements using paramagnetic spin labels / David Eliezer -- Magic angle spinning solid-state NMR experiments for structural characterization of proteins / Lichi Shi, Vladimir Ladizhansky -- Wide-line NMR and protein hydration / K. Tompa, M. Bokor, P. Tompa -- 5-Fluoro-D,L-Tryptophan as a dual NMR and fluorescent probe of Ü-synuclein / Candace M. Pfefferkorn, Jennifer C. Lee -- Alpha proton detection based backbone assignment of intrinsically disordered proteins / Perttu Permi, Maarit Hellman -- Fourier transform infrared spectroscopy of intrinsically disordered proteins : measurement procedures and data analyses / Antonino Natalello, Diletta Ami, Silvia Maria Doglia -- Monitoring structural transitions in IDPs by vibrational spectroscopy of cyanylated systeine / Hailiu Yang ... [et al.] -- Structure analysis of unfolded peptides I : vibrational circular dichroism spectroscopy / Reinhard Schweitzer-Stenner, Jonathan B. Soffer, Daniel Verbaro -- Structural analysis of unfolded peptides by raman spectroscopy / Reinhard Schweitzer-Stenner ... [et al.] -- Isotope-edited infrared spectroscopy / Ginka S. Buchner, Jan Kubelka -- Monitoring structural transitions in IDPs by site-directed spin labeling EPR spectroscopy / Johnny Habchi ... [et al.] -- Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains / Lucia B. Chemes ... [et al.] -- Deconstructing time-resolved optical rotatory dispersion kinetic measurements of cytochrome c folding : from molten globule to the native state / Eefei Chen, David S. Kliger -- Use of UV-Vis absorption spectroscopy for studies of natively disordered proteins / Eugene A. Permyakov -- Intrinsic fluorescence of intrinsically disordered proteins / Paolo Neyroz, Stefano Ciurli -- Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states / Anna I. Sulatskaya ... [et al.] -- Fluorescence lifetime measurements of intrinsically unstructured proteins : application to Ü-synuclein / Sarah Schreurs ... [et al.] -- Ensemble FRET methods in studies of intrinsically disordered proteins / Elisha Haas -- Fluorescence correlation spectroscopy to determine the diffusion coefficient of Ü-synuclein and follow early oligomer formation / Sangeeta Nath, Manli Deng, Yves Engelborghs.