Intrinsically Disordered Protein Analysis

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