(1) Biophysics Graduate Group, University of California, Davis, CA 95616, USA;(2) L-448 Biosciences Director ate, Lawrence Livermore National Laboratory, Livermore, CA 94551, USA
Abstract:
We have recently shown that the averaged chemical shift (ACS) of a nucleus in the protein backbone correlates well empirically to its secondary structure content (SSC). This allows the estimation of SSC directly from the NMR spectrum without the time intensive process of chemical shift assignment. Here, we present an empirical correlation that accounts both for contributions to the relevant protein and chemical shift databases made subsequent to the original analysis, and for missing or inconsistently referenced resonances. Our results affirm that this method provides a significant tool for initial structural prediction from NMR data prior to complete chemical shift assignment.
