Intrinsically disordered protein analysis. Volume 1, Methods and experimental tools /
Intrinsically disordered protein analysis. Volume 1, Methods and experimental tools /
Methods and experimental tools
edited by Vladimir N. Uversky, A. Keith Dunker.
- New York : Humana Press : Springer, ©2012.
- 1 online resource (xiv, 511 pages) : illustrations (some color)
- Methods in molecular biology, 895 1940-6029 ; .
- Methods in molecular biology (Clifton, N.J.) ; v. 895. .
Includes bibliographical references and index.
Determination of IUP based on susceptibility for degradation by default / In-cell NMR of intrinsically disordered proteins in prokaryotic cells / In-cell NMR in Xenopus laevis oocytes / In-cell NMR in mammalian cells : part 1 / In-cell NMR in mammalian cells : part 2 / In-cell NMR in mammalian cells : part 3 / Fourier transform infrared microspectroscopy of complex biological systems : from intact cells to whole organisms / Studying IDP stability and dynamics by fast relaxation imaging in Living Cells / Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered Proteins / Distance information for disordered proteins from NMR and ESR measurements using paramagnetic spin labels / Magic angle spinning solid-state NMR experiments for structural characterization of proteins / Lichi Shi, Vladimir Ladizhansky -- Wide-line NMR and protein hydration / 5-Fluoro-D,L-Tryptophan as a dual NMR and fluorescent probe of Ü-synuclein / Alpha proton detection based backbone assignment of intrinsically disordered proteins / Fourier transform infrared spectroscopy of intrinsically disordered proteins : measurement procedures and data analyses / Monitoring structural transitions in IDPs by vibrational spectroscopy of cyanylated systeine / Structure analysis of unfolded peptides I : vibrational circular dichroism spectroscopy / Structural analysis of unfolded peptides by raman spectroscopy / Isotope-edited infrared spectroscopy / Monitoring structural transitions in IDPs by site-directed spin labeling EPR spectroscopy / Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains / Deconstructing time-resolved optical rotatory dispersion kinetic measurements of cytochrome c folding : from molten globule to the native state / Use of UV-Vis absorption spectroscopy for studies of natively disordered proteins / Intrinsic fluorescence of intrinsically disordered proteins / Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states / Fluorescence lifetime measurements of intrinsically unstructured proteins : application to Ü-synuclein / Ensemble FRET methods in studies of intrinsically disordered proteins / Fluorescence correlation spectroscopy to determine the diffusion coefficient of Ü-synuclein and follow early oligomer formation / Peter Tsvetkov, Yosef Shaul -- Yutaka Ito, Tsutomu Mikawa, Brian O. Smith -- Rossukon Thongwichian, Philipp Selenko -- Beata Bekei ... [et al.] -- Beata Bekei ... [et al.] -- Beata Bekei ... [et al.] -- Diletta Ami, Antonino Natalello, Silvia Maria Doglia -- Apratim Dhar ... [et al.] -- Loic Salmon ... [et al.] -- David Eliezer -- K. Tompa, M. Bokor, P. Tompa -- Candace M. Pfefferkorn, Jennifer C. Lee -- Perttu Permi, Maarit Hellman -- Antonino Natalello, Diletta Ami, Silvia Maria Doglia -- Hailiu Yang ... [et al.] -- Reinhard Schweitzer-Stenner, Jonathan B. Soffer, Daniel Verbaro -- Reinhard Schweitzer-Stenner ... [et al.] -- Ginka S. Buchner, Jan Kubelka -- Johnny Habchi ... [et al.] -- Lucia B. Chemes ... [et al.] -- Eefei Chen, David S. Kliger -- Eugene A. Permyakov -- Paolo Neyroz, Stefano Ciurli -- Anna I. Sulatskaya ... [et al.] -- Sarah Schreurs ... [et al.] -- Elisha Haas -- Sangeeta Nath, Manli Deng, Yves Engelborghs.
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.
9781617799273 1617799270 1617799262 9781617799266
10.1007/978-1-61779-927-3 doi 9781617799266
9781617799266 00012511
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
Laboratory Manual
Laboratory manuals
Laboratory manuals.
Manuels de laboratoire.
QP551 / .I58 2012 QP551 / .I627 2012 v.1
572/.6
Includes bibliographical references and index.
Determination of IUP based on susceptibility for degradation by default / In-cell NMR of intrinsically disordered proteins in prokaryotic cells / In-cell NMR in Xenopus laevis oocytes / In-cell NMR in mammalian cells : part 1 / In-cell NMR in mammalian cells : part 2 / In-cell NMR in mammalian cells : part 3 / Fourier transform infrared microspectroscopy of complex biological systems : from intact cells to whole organisms / Studying IDP stability and dynamics by fast relaxation imaging in Living Cells / Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered Proteins / Distance information for disordered proteins from NMR and ESR measurements using paramagnetic spin labels / Magic angle spinning solid-state NMR experiments for structural characterization of proteins / Lichi Shi, Vladimir Ladizhansky -- Wide-line NMR and protein hydration / 5-Fluoro-D,L-Tryptophan as a dual NMR and fluorescent probe of Ü-synuclein / Alpha proton detection based backbone assignment of intrinsically disordered proteins / Fourier transform infrared spectroscopy of intrinsically disordered proteins : measurement procedures and data analyses / Monitoring structural transitions in IDPs by vibrational spectroscopy of cyanylated systeine / Structure analysis of unfolded peptides I : vibrational circular dichroism spectroscopy / Structural analysis of unfolded peptides by raman spectroscopy / Isotope-edited infrared spectroscopy / Monitoring structural transitions in IDPs by site-directed spin labeling EPR spectroscopy / Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains / Deconstructing time-resolved optical rotatory dispersion kinetic measurements of cytochrome c folding : from molten globule to the native state / Use of UV-Vis absorption spectroscopy for studies of natively disordered proteins / Intrinsic fluorescence of intrinsically disordered proteins / Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states / Fluorescence lifetime measurements of intrinsically unstructured proteins : application to Ü-synuclein / Ensemble FRET methods in studies of intrinsically disordered proteins / Fluorescence correlation spectroscopy to determine the diffusion coefficient of Ü-synuclein and follow early oligomer formation / Peter Tsvetkov, Yosef Shaul -- Yutaka Ito, Tsutomu Mikawa, Brian O. Smith -- Rossukon Thongwichian, Philipp Selenko -- Beata Bekei ... [et al.] -- Beata Bekei ... [et al.] -- Beata Bekei ... [et al.] -- Diletta Ami, Antonino Natalello, Silvia Maria Doglia -- Apratim Dhar ... [et al.] -- Loic Salmon ... [et al.] -- David Eliezer -- K. Tompa, M. Bokor, P. Tompa -- Candace M. Pfefferkorn, Jennifer C. Lee -- Perttu Permi, Maarit Hellman -- Antonino Natalello, Diletta Ami, Silvia Maria Doglia -- Hailiu Yang ... [et al.] -- Reinhard Schweitzer-Stenner, Jonathan B. Soffer, Daniel Verbaro -- Reinhard Schweitzer-Stenner ... [et al.] -- Ginka S. Buchner, Jan Kubelka -- Johnny Habchi ... [et al.] -- Lucia B. Chemes ... [et al.] -- Eefei Chen, David S. Kliger -- Eugene A. Permyakov -- Paolo Neyroz, Stefano Ciurli -- Anna I. Sulatskaya ... [et al.] -- Sarah Schreurs ... [et al.] -- Elisha Haas -- Sangeeta Nath, Manli Deng, Yves Engelborghs.
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.
9781617799273 1617799270 1617799262 9781617799266
10.1007/978-1-61779-927-3 doi 9781617799266
9781617799266 00012511
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
Laboratory Manual
Laboratory manuals
Laboratory manuals.
Manuels de laboratoire.
QP551 / .I58 2012 QP551 / .I627 2012 v.1
572/.6