Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins

Biochem Soc Trans. 2012 Oct;40(5):1014-20. doi: 10.1042/BST20120171.


NMR spectroscopy offers the unique possibility to relate the structural propensities of disordered proteins and loop segments of folded peptides to biological function and aggregation behaviour. Backbone chemical shifts are ideally suited for this task, provided that appropriate reference data are available and idiosyncratic sensitivity of backbone chemical shifts to structural information is treated in a sensible manner. In the present paper, we describe methods to detect structural protein changes from chemical shifts, and present an online tool [ncSPC (neighbour-corrected Structural Propensity Calculator)], which unites aspects of several current approaches. Examples of structural propensity calculations are given for two well-characterized systems, namely the binding of α-synuclein to micelles and light activation of photoactive yellow protein. These examples spotlight the great power of NMR chemical shift analysis for the quantitative assessment of protein disorder at the atomic level, and further our understanding of biologically important problems.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Micelles
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Photoreceptors, Microbial / chemistry*
  • Photoreceptors, Microbial / metabolism
  • Protein Conformation
  • alpha-Synuclein / chemistry*
  • alpha-Synuclein / metabolism


  • Bacterial Proteins
  • Micelles
  • Photoreceptors, Microbial
  • alpha-Synuclein
  • photoactive yellow protein, Bacteria