This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for 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.