We have developed a set of tools for rapidly mapping disufide bonds in proteins. The strategy involves extensive cleavage of the protein of interest with enzymes under conditions that prevent breakage or interchange of disulfide linkages; followed by analysis of the resulting fragments by MALDIion trap mass spectrometry. We have used the technique to successfully map growth factors, proteinaceous toxins, and an analogue of the human LDL receptor. A paper describing this work has been published (Qin and Chait, Anal. Chem. 69,4002-4009, 1997).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000862-27
Application #
6307559
Study Section
Project Start
1999-12-01
Project End
2000-11-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
27
Fiscal Year
2000
Total Cost
$8,199
Indirect Cost
Name
Rockefeller University
Department
Type
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
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