Application of Solution nmr spectroscopy to Study Protein Dynamics

2012

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It is not clear if the insights from calmodulin binding events can be generalized, but the potential of 

experimentally decompose the overall entropy into its individual components is remarkable. With this 

method, energetic contributions to binding events can be studied in a detailed, residue specific manner.  

The above over-simplified characterization of fluctuations and dynamics based on their different 

time scales that can be studied by NMR in reality often are not very clear-cut. There are situations 

where contributions from dynamics at different time scales overlap. Typically, in these cases only the 

upper or lower limits of the motions can be defined. Interestingly, there are other NMR parameters that 

envelope the full range of time scales, from nanoseconds all the way to seconds.