Intrinsically Disordered Protein Analysis
Springer-Verlag New York Inc.
978-1-4614-3703-1 (ISBN)
Thorough and intuitive, Intrinsically Disordered Protein Analysis: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules.
Immobilization of Proteins for Single Molecule Fluorescence Resonance Energy Transfer Measurements of Conformation and Dynamics.-Application of Confocal Single Molecule FRET to Intrinsically Disordered Proteins.-Single-Molecule Force Spectroscopy of Chimeric Polyprotein Constructs Containing Intrinsically Disordered Domains.-Visualization of Mobility by Atomic Force Microscopy.-Unequivocal Single-Molecule Force Spectroscopy of Intrinsically Disordered Proteins.-Sedimentation Velocity Analytical Ultracentrifugation for Intrinsically Disordered Proteins.-Analysis of Intrinsically Disordered Proteins by Small-Angle X-ray Scattering.-Small Angle Neutron Scattering (SANS) for the Structural Study of Intrinsically Disordered Proteins in Solution: a Practical Guide.-Dynamic and Static Light Scattering of Intrinsically Disordered Proteins.-Estimation of Intrinsically Disordered Protein Shape and Time-averaged Apparent Hydration in Native Conditions by a Combination of Hydrodynamic Methods.-Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins.-Denaturant-induced Conformational Transitions in Intrinsically Disordered Proteins.-Identification of Intrinsically Disordered Proteins by a Special 2D Electrophoresis.-pH-induced Changes in Intrinsically-disordered Proteins.-Temperature Induced Transitions in Disordered Proteins Probed by NMR Spectroscopy.-Analyzing Temperature Induced Transitions in Disordered Proteins by NMR Spectroscopy and Secondary Chemical Shift Analyses.-Osmolyte-, Binding-, and Temperature-Induced Transitions of Intrinsically Disordered Proteins.-Laser Temperature-jump Spectroscopy of Intrinsically Disordered Proteins.-Differential Scanning Microcalorimetry of Intrinsically Disordered Proteins.-Identifying Disordered Regions in Proteins by Limited Proteolysis.-The Effect of Counter Ions on the Conformation of Intrinsically Disordered Proteins Studied by Size-exclusion Chromatography.-Mean Net Charge of Intrinsically Disordered Proteins: Experimental Determination of Protein Valence by Electrophoretic Mobility Measurements.-Protein Characterization by Partitioning in Aqueous Two-Phase Systems.-Detection and Characterization of Large-scale Protein Conformational Transitions in Solution using Charge-state Distribution Analysis in ESI-MS.-Localizing Flexible Regions in Proteins using Hydrogen Deuterium Exchange Mass Spectrometry.-Mass-spectrometry Tools for Analysis of Intermolecular Interactions.-Characterization of Oligomerization- Aggregation Products of Neurodegenerative Target Proteins by Ion Mobility Mass Spectrometry.-Identifying Solubility-promoting Buffers for Intrinsically Disordered Proteins Prior to Purification.-Proteomic Methods for the Identification of Intrinsically Disordered Proteins.-Selective Isotope Labeling of Recombinant Proteins in E. coli.
Erscheint lt. Verlag | 21.7.2012 |
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Reihe/Serie | Methods in Molecular Biology ; 896 |
Zusatzinfo | XIV, 454 p. |
Verlagsort | New York, NY |
Sprache | englisch |
Maße | 178 x 254 mm |
Themenwelt | Naturwissenschaften ► Biologie ► Biochemie |
Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie | |
ISBN-10 | 1-4614-3703-2 / 1461437032 |
ISBN-13 | 978-1-4614-3703-1 / 9781461437031 |
Zustand | Neuware |
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