Monitoring Protein Folding Using Time-Resolved Biophysical Techniques
Many of the biophysical techniques developed to characterize native proteins at equilibrium have now been adapted to the structural and thermodynamic characterization of transient species populated during protein folding. Recent advances in these techniques, the use of novel methods of initiating refolding, and a convergence of theoretical and experimental approaches are leading to a detailed understanding of many aspects of the folding process.
KeywordsAnisotropy Tyrosine Amide Cysteine Iodide
chymotrypsin inhibitor 2
chemically induced dynamic nuclear polarization
nuclear Overhauser effect
nuclear magnetic resonance
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