To be confirmed

I will present the analysis of a Molecular Dynamics study on solvated glutamate, one of the 20 proteinogenic amino acids. Glutamate has gained media interest in recent years due to the use of mono sodium glutamate as a flavour enhancer in food and the associated health risks. Although it is essential for proteins and is the most abundant excitory neurotransmitter, an extra-cellular build up of glutamate has been associated with various neuroendocrine and neurological disorders, although much of this is poorly understood. Thus a combination of experimental and computer simulation is needed to understand glutamate so that we can build a better picture of why glutamate outside proteins can be dangerous. A recent study (E.J.M. Leenders et al., J. Chem. Theory Comput. 4, 898 (2008)) discussed the water-glutamate interactions, however no work has been done on glutamate-glutamate interactions in solution. Our work aims to build on this, focusing on the glu-glu interactions instead of the solute-solvent effects. We found a marked difference in the behaviour of the two carboxylate groups on glutamate, particularly with the side-chain showing a greater propensity to form bifurcated bonds. I will therefore present a discussion of the structural properties of the two carboxylate groups of glutamate molecules in aqueous solution.