This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The 26-amino acid peptide melittin is a primary component of honeybee venom, and is produced in two forms by the organism: a form with a charged N-terminus (NH3+) and a form where the N-terminus is formylated. Melittin is highly helical and it is thought that the peptide secondary structure plays a key role in melittins ability to participate in hemolysis. This study is undertaken to understand whether the N-formylation has a profound effect on the solution secondary structure of the peptide, and whether the observed differences in secondary structure are force-field dependent.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR006009-17
Application #
7601521
Study Section
Special Emphasis Panel (ZRG1-BCMB-Q (40))
Project Start
2007-08-01
Project End
2008-07-31
Budget Start
2007-08-01
Budget End
2008-07-31
Support Year
17
Fiscal Year
2007
Total Cost
$299
Indirect Cost
Name
Carnegie-Mellon University
Department
Biostatistics & Other Math Sci
Type
Schools of Arts and Sciences
DUNS #
052184116
City
Pittsburgh
State
PA
Country
United States
Zip Code
15213
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