Characterization of a C-terminal fragment of the recombinant STAT1 protein by MALDI-MS. Determination of the extent of alkylation as well as phosphorylation of the protein. Continuation of this project will include the determination of amino acid residues that are important for DNA binding using photocrosslinking and MALDI-MS peptide mapping. A paper describing this work has been published U. Vinkemeier, S.L. Cohen. I. Moarefi, B.T. Chait, J. Kuriyan & J.E. Darnell """"""""DNA binding of in vitro activated Stat1(, Stat1( and truncated Stat1 interaction between NH2-terminal domains stabilizes binding of two dimers to tandem DNA sites."""""""" EMBO J. 15 (1996) 5616 - 5626.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000862-25
Application #
6279462
Study Section
Project Start
1997-12-01
Project End
1998-11-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
25
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Rockefeller University
Department
Type
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
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