Secondary structure of proteins from chemical shifts


The systematic conformation dependence of 13C chemical shifts in proteins provides useful structural insights even for ‘difficult’ proteins that do not crystallize or dissolve. Taking advantage of >1.2 million 13C chemical shifts in the Biological Magnetic Resonance (data)Bank, we have determined the characteristic chemical shift ranges of α-helix, β-sheet and random-coil of the 20 canonical amino acids. This required identification and removal of ~14% incorrectly referenced or otherwise compromised datasets. The purged data reveal unusual structural features, such as distinct chemical shifts associated with “left-handed helix” conformations.


  1. Keith J. Fritzsching # , Mei Hong and Klaus Schmidt-Rohr # "Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria" J. Biomol. NMR 64: 115-130 (2016).