Abstract
Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970-2978, 2001). The chemical shifts are determined at neutral pH in order to match the conditions of most studies of intrinsically disordered proteins. Temperature has a non-negligible effect on the (13)C random coil chemical shifts, so temperature coefficients are reported for the random coil chemical shifts to allow extrapolation to other temperatures. The pH dependence of the histidine random coil chemical shifts is investigated in a titration series, which allows the accurate random coil chemical shifts to be obtained at any pH. By correcting the random coil chemical shifts for the effects of temperature and pH, systematic biases of the secondary chemical shifts are minimized, which will improve the reliability of detection of transient secondary structure in disordered proteins.
| Original language | English |
|---|---|
| Journal | Journal of Biomolecular NMR |
| Volume | 49 |
| Issue number | 2 |
| Pages (from-to) | 139-49 |
| Number of pages | 11 |
| ISSN | 0925-2738 |
| DOIs | |
| Publication status | Published - Feb 2011 |
Keywords
- Hydrogen-Ion Concentration
- Nuclear Magnetic Resonance, Biomolecular
- Protein Folding
- Proteins
- Temperature