A project has been initiated to study the structure of two small heat shock proteins The sHSP's are ubiquitous among eukaryotes and are hypothesized to be a new class of molecular chaperone. The initial studies are with pea HSP 18. 1 and its S. cerevisiae homologue HSP26. Both proteins are small (18.1 kDa and -23 kDa respectively) but appear to exist as large homo-oligomers. From sedimentation and size-exclusion chromatography, the oligomer of the HSPI 8.1 could be a dodecamer and the HSP26 could be a 24-mer. Preliminary experiments are promising, although there is a large background of denatured protein film winch is common for tins type of protein. Further work will involve fixation of the protein and/or pretreatment of the carbon film substrate. We have been concentrating on the Hsp 26 winch behaves somewhat better thari the Hsp 18. 1. A brief glutaraldehyde fixation prior to deposition on the grid seems to help, but the optimal conditions have not yet been attained.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001777-19
Application #
6444666
Study Section
Project Start
2001-04-01
Project End
2002-09-29
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
19
Fiscal Year
2001
Total Cost
$293,069
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
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