PEPTITERGENTS: NOVEL PEPTIDES CAPABLE OF SOLUBILIZING MEMBRANE PROTEINS FOR CRYSTALLIZATION. Robert M. Stroud and Christian Schafmeister, S-964 Dept. of Biochemistry & Biophysics UCSF Box 0448 San Francisco, CA 94143-0448

Peptides that form [[alpha]]-helices with a strongly amphipathic nature are capable of solubilizing membrane proteins if they fulfill certain criteria. Adequate length, a flat hydrophobic surface, and a polar exterior are the main components of these peptides. Variations in the initial peptide structure have been made and resulted in many variations on the original theme. The crystal structure of the initial peptide used to solubilize membrane proteins is described and shows the nature of the interface between hydrophobic surfaces and laterally between adjacent membrane-spanning peptitergents. The crystal structure was solved entirely from [[alpha]]-helical models using molecular replacement.