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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6322192
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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