Nuclear magnetic resonance denatured proteins

One of the primary mechanisms of protein degradation is the loss of globular structure [118, 119]. This process, termed denaturation, leads to a partially or completely unfolded species which usually lacks any of the biological activity of the native protein. A variety of methods have been employed to monitor the denaturation of proteins, including fluorescence, infrared, nuclear magnetic resonance (NMR), and CD spectroscopy. As CD is very sensitive to changes in both secondary and tertiary structure, its application to the study of protein folding... 

R 313 D. Shortle, The Expended Denatured State An Ensemble of Conformations Trapped in a Locally Encoded Topological Space , p. 1 R 314 H.J. Dyson and P.E. Wright, Insights into the Structure and Dynamics of Unfolded Proteins from Nuclear Magnetic Resonance , p. 311... 

Structural information on proteins can be obtained with X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy however, due to various limitations intrinsic to these high-resolution structmal methods, only alternate spectroscopic techniques (especially fluorescence, circular dichroism (CD), Raman, and infrared spectroscopic techniques) can be employed for conformational characterization of proteins as well as stabilization and denaturation of enzymes. 

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