Methyl group assignment using pseudocontact shifts with PARAssign

J Biomol NMR. 2017 Dec;69(4):183-195. doi: 10.1007/s10858-017-0136-3. Epub 2017 Nov 27.

Abstract

A new version of the program PARAssign has been evaluated for assignment of NMR resonances of the 76 methyl groups in leucines, isoleucines and valines in a 25 kDa protein, using only the structure of the protein and pseudocontact shifts (PCS) generated with a lanthanoid tag at up to three attachment sites. The number of reliable assignments depends strongly on two factors. The principle axes of the magnetic susceptibility tensors of the paramagnetic centers should not be parallel so as to avoid correlated PCS. Second, the fraction of resonances in the spectrum of a paramagnetic sample that can be paired with the diamagnetic counterparts is critical for the assignment. With the data from two tag positions a reliable assignment could be obtained for 60% of the methyl groups and for many of the remaining resonances the number of possible assignments is limited to two or three. With a single tag, reliable assignments can be obtained for methyl groups with large PCS near the tag. It is concluded that assignment of methyl group resonances by paramagnetic tagging can be particularly useful in combination with some additional data, such as from mutagenesis or NOE-based experiments. Approaches to yield the best assignment results with PCS generating tags are discussed.

Keywords: Assignment; Heat shock protein; Methyl groups; NMR spectroscopy; Paramagnetic tag; Pseudocontact shift.

MeSH terms

  • Heat-Shock Proteins / chemistry
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Proteins / chemistry*

Substances

  • Heat-Shock Proteins
  • Proteins