  We present a detailed heuristic method to quantify the degree of local
energetic frustration manifested by protein molecules. Current applications are
realized in computational experiments where a protein structure is visualized
highlighting the energetic conflicts or the concordance of the local
interactions in that structure. Minimally frustrated linkages highlight the
stable folding core of the molecule. Sites of high local frustration, in
contrast, often indicate functionally relevant regions such as binding, active
or allosteric sites.
