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. Snapshot from a simulation of liquid water. ... Impact of a drop of water. ... Dehydration (hypohydration) is the removal of water (hydor in ancient Greek) from an object. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Dehydration is the removal of water (hydor in ancient Greek) from an object. ... Amide functional group In chemistry, an amide is one of two kinds of compound. ... Carbonyl group In organic chemistry, a carbonyl group is a functional group composed of a carbon atom double-bonded to an oxygen atom. ... In chemistry, a hydrogen bond is a type of attractive intermolecular force that exists between two partial electric charges of opposite polarity. ... In chemistry, a nonpolar compound is one that does not have concentrations of positive or negative electric charge. ... ... Proteins are amino acid chains, made up from 20 different L-α-amino acids, also referred to as residues, that fold into unique three-dimensional protein structures. ... Websites A sticky website is one that visitors return to repeatedly. ... Impact of a drop of water. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... In chemistry, a ligand is an atom, ion, or molecule (see also: functional group) that generally donates one or more of its electrons through a coordinate covalent bond to, or shares its electrons through a covalent bond with one or more central atoms or ions (these ligands act as a... Electrostatics is the branch of physics that deals with the force exerted by a static (i. ... Interaction is a kind of action which occurs as two or more objects have an effect upon one another. ... Amide functional group In chemistry, an amide is one of two kinds of compound. ... Carbonyl group In organic chemistry, a carbonyl group is a functional group composed of a carbon atom double-bonded to an oxygen atom. ... There are a number of uses for the word shield: A shield is a protective device, meant to intercept attacks. ... Look up charge in Wiktionary, the free dictionary. ... Snapshot from a simulation of liquid water. ... Nonbonded interactions are interactions through electrostatic or van der Waals forces between atoms that are not directly bonded together. ... Look up charge in Wiktionary, the free dictionary. ... Dehydration (hypohydration) is the removal of water (hydor in ancient Greek) from an object. ... This article or section does not cite its references or sources. ... ‹ The template below has been proposed for deletion. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Oral medication Caffeine is the most widely used psychoactive substance in the world. ...

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).