SMALL ORGANOMETALLIC COMPLEXES IN PROTEIN FOLDING

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We are currently investigating the role of small organometallic complexes in protein folding. Our preliminary studies indicate that these species can have a significant influence on the path and rate of protein folding. Specifically, these complexes can slow or halt the folding of a protein under folding conditions. This folding process is normally complete within a few seconds in the absence of the metal complex. The role of chaperones like GroEl/Es in cellular folding is well-documented. We believe that these organometallics may slow the process of mis-folding and aggregatioin in newly created proteins, allowing time for the cell to transport these proteins to GroE-type proteins. In some cases, these complexes may directly assist in the folding process by inhibiting an otherwise fast misfolding process but permitting a more energetic, slow, correct folding. Our current means of assessing these phenomena are indirect. A direct measure of the radius of these complexes will greatly assist in our research.