Biophysical characterization of intrinsically disordered proteins.
The challenges associated with the structural characterization of disordered proteins have resulted in the application of a host of biophysical methods to such systems. NMR spectroscopy is perhaps the most readily suited technique for providing high-resolution structural information on disordered protein states in solution. Optical methods, solid state NMR, ESR and X-ray scattering can also provide valuable information regarding the ensemble of conformations sampled by disordered states. Finally, computational studies have begun to assume an increasingly important role in interpreting and extending the impact of experimental data obtained for such systems. This article discusses recent advances in the applications of these methods to intrinsically disordered proteins.
Eliezer
David
D
Weill Cornell Medical College, 1300 York Avenue, New York, NY 10065, United States. dae2005@med.cornell.edu
D000818:Animals; D001703:Biophysics / Q000379:methods*; D019295:Computational Biology; D018360:Crystallography, X-Ray; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins