As an integral part of our structural studies of proteins we routinely need to oxidatively fold polypeptides. Both synthesized peptides and proteins cytoplasmically expressed in vivo do not form disulfide bonds. In a number of cases our lab is intensively working out the in vitro conditions necessary for formation of the native disulfide bonding pattern. Analysis of these efforts would be greatly accelerated by the ability to quickly and accurately determine the weight of the products of such reactions. This information will allow us to watch the removal of blocking groups (on synthesized polypeptides), check for unwanted labeling of labile residues withoxidative agents (such as iodine), and, if possible, determine the relative amounts of SH and S-S groups.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001614-17
Application #
6281196
Study Section
Project Start
1998-03-01
Project End
1999-02-28
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
17
Fiscal Year
1998
Total Cost
Indirect Cost
Name
University of California San Francisco
Department
Type
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143
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