Abstract
The known protonation states of protein crystal structures obtained using X-ray and neutron crystallographic data, and including relevant NMR derived experimental information, have been predicted using three pKa calculation tools, namely PROPKA, H++ and MCCE. Comparisons between the experimental and predicted protonation states have been carried out in order to assess whether the results are of sufficient quality to validate their use in predicting the protonation states of two key histidine residues in the lobster carapace colouration protein β-crustacyanin as an example. Significant interest has been shown in the protonation states of these residues, which have been out of reach of experiment thus far and are likely to remain so.
Original language | English |
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Pages (from-to) | 231-259 |
Number of pages | 28 |
Journal | Crystallography Reviews |
Volume | 15 |
Issue number | 4 |
DOIs | |
Publication status | Published - Oct 2009 |
Keywords
- Amino acids
- Neutron crystallography
- NMR
- Protein pKa predictions
- Protonation states
- X-ray crystallography