title: Comparing the structural topology of integral and peripheral membrane proteins utilizing electron paramagnetic resonance spectroscopy.
abstract: The alignment of membrane proteins provides pertinent structural and dynamic information. Structural topology data gleaned from such studies can be used to determine the functional mechanisms associated with a wide variety of integral membrane proteins. In this communication, we successfully demonstrate, for the first time, the determination of the structural topology and helical tilt of an antimicrobial peptide magainin 2 using aligned X-band spin-label EPR spectroscopic techniques. This novel comparison unlocks many possibilities utilizing EPR spectroscopy to probe antimicrobial peptide topologies with increased sensitivity and may also give further clues to elucidate their corresponding mechanisms.
authors.affiliation: Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA.
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Mayo
authors.forename: Johnson J
authors.initials: JJ
authors.lastname: Inbaraj
authors.forename: Nidhi
authors.initials: N
authors.lastname: Subbaraman
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Grosser
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Chan
authors.forename: Gary A
authors.initials: GA
authors.lastname: Lorigan
mesh_terms: D000595:Amino Acid Sequence; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D008051:Lipid Bilayers / Q000737:chemistry; D054806:Magainins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011976:Receptors, Muscarinic / Q000737:chemistry; D016415:Sequence Alignment
chemical_list: D008051:Lipid Bilayers; D054806:Magainins; D011976:Receptors, Muscarinic