SMALL ORGANOMETALLIC COMPLEXES IN PROTEIN FOLDING

我们目前正在研究小的有机金属的作用 蛋白质折叠中的复合物。 我们的初步研究表明， 这些物种可以对路径和速率产生重大影响， 蛋白质折叠 具体来说，这些复合物可以减缓或停止 蛋白质在折叠条件下的折叠。 这个折叠过程 在没有金属的情况下通常在几秒钟内完成 复杂. 分子伴侣如GroEl/Es在细胞折叠中的作用是 记录良好 我们相信这些有机金属化合物可以减缓 在新产生的蛋白质中错误折叠和聚集的过程， 使细胞有时间将这些蛋白质转运到GroE型 proteins. 在某些情况下，这些复合物可以直接帮助 通过抑制否则快速的错误折叠过程， 允许更有力、缓慢、正确的折叠。 我们目前的手段 对这些现象的评估是间接的。 的直接量度 这些配合物的半径将大大有助于我们的研究。

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.