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Full Description
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.
Contents
Determination of IUP Based on Susceptibility for Degradation by Default.-In-cell NMR of Intrinsically Disordered Proteins. 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.-Using Chemical Shifts to Assess Transient Secondary Structure and Generate Ensemble Structures of Intrinsically Disordered Proteins.-Magic Angle Spinning Solid State NMR Experiments for Structural Characterization of Proteins.-Wide-line NMR and Protein Hydration.-5-Fluorotryptophan as a Dual NMR and Fluorescent Probe of a-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 Stuctural Transitions in IDPs by Vibrational Spectroscopy of Cyanlated Cysteine.-Structure Analysis of Unfolded Peptides by Vibrational Circular DichroismSpectroscopy.-Structural Analysis of Unfolded Peptides by Raman Spectroscopy.-Isotope-Edited Infrared Spectroscopy.-MONITORING STRUCTURAL TRANSITIONS IN IDPs BY SITE-DIRECTED SPINLABELING 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.-The use of UV-VIS Absorption Spectroscopy for Analysis of Natively Disordered Proteins.-Intrinsic Fluorescence of Intrinsically Disordered Proteins.-Binding Stoichiometry and Affinity of Fluorescent Dyes to Proteins in Different Structural States.-Fluoresence Lifetime Measurements of Intrinsically Unstructured Proteins-Application to a-Synuclein.-Ensemble FRET Methods in Studies of Intrinsically Disordered Proteins.-Fluorescence Correlation Spectroscopy to Determine the Diffusion Coefficient of a-Synuclein and Follow Early Oligomer Formation.
