Benefits

• When the behavior of proteins in a solution is examined by spectral density mapping, the results are of higher quality than with other forms of analysis. Regardless of the field strength used in the NMRS, spectral density mapping has historically provided the most consistently clear images for analysis.
  
  

Errors

• System errors, especially in measurement, can occur in spectral density mapping. Error measurement is completed by testing how much relaxation the chains of nuclei experience during experiments. The length and width of relaxation are given a corresponding number and letter. 15N relaxation, for example, has provided little margin of error. In another measurement, 13C relaxation is less accurate and can vary, depending on the type of motion of created by the protein molecules.
  
  

Considerations

• In the analysis of proteins, traditional spectral density mapping using spectrometer measuring was time-consuming. In 2007, a technique was developed to reduce the time necessary for high quality spectral densities by about half that of previous methods.