Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins.

Produktinformation

Utgivningsdatum2016-08-23
Mått178 x 254 x undefined mm
FormatHäftad
SpråkEngelska
SerieMethods in Molecular Biology
Antal sidor511
FörlagHumana Press Inc.
ISBN9781493962303

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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.

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Intrinsically Disordered Protein Analysis

Volume 1, Methods and Experimental Tools

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AvVladimir N. Uversky,A. Keith Dunker

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Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins.

Produktinformation

Utgivningsdatum2016-08-23
Mått178 x 254 x undefined mm
FormatHäftad
SpråkEngelska
SerieMethods in Molecular Biology
Antal sidor511
FörlagHumana Press Inc.
ISBN9781493962303

Tillhör följande kategorier

Biokemi inom Naturvetenskap och teknik

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.

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Finns i fler format (3)

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