Dehydron
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A dehydron is an intramolecular hydrogen bond poorly shielded from water attack, with a propensity to promote its own dehydration. Dehydrons are a special kind of packing defects in soluble proteins named and characterized in a number of research papers by Ariel Fernandez, from Rice University, and his coworkers Ridgway Scott, Stephen Berry and Harold Scheraga.
Dehydrons are partially dehydrated amide-carbonyl hydrogen bonds that result from an incomplete clustering of nonpolar groups wrapping the polar pair within the protein structure. Dehydrons are sticky, since they promote the removal of surrounding water through protein associations and/or ligand binding. This further dehydration enhances the electrostatic interaction between the amide and carbonyl groups by de-shielding their partial charges. Furthermore, the dehydration stabilizes the hydrogen bond by destabilizing the nonbonded state that consists of dehydrated isolated charges. Hence, the name dehydron makes reference to the tendency to promote its dehydration, a process both energetically and thermodynamically favored. Thus, dehydrons are markers for protein interactivity, and hence functional indicators, and may possibly serve as drug targets.
[edit] References:
- Fernandez, A. and Scott, L. R. Biophys. J. 85, 1914-1928 (2003).
- Fernandez, A. and Scheraga, H. A. Proc. Natl. Acad. Sci. USA 100, 113-118 (2003).
- Fernandez, A. and Scott, L. R. Phys. Rev. Lett. 91, 08102 (2003).
- Fernandez, A., Rogale, K., Scott, L. R. and Scheraga, H. A. Proc. Natl. Acad. Sci. USA 101, 11640-11645 (2004).
- Fernandez, A. and Berry, R. S. Proc. Natl. Acad. Sci. USA 101, 13460-13465 (2004).
- Fernandez, A. Nature Biotechnology 22, 1081-1085 (2004).
- Fernandez, A. Structure 13, 1829-1836 (2005).
