title: 14N Polarization Inversion Spin Exchange at Magic Angle (PISEMA).
abstract: Polarization Inversion Spin Exchange at Magic Angle (PISEMA) is a powerful experiment for determining peptide orientation in uniformly aligned samples such as planar membranes. In this paper, we present (14)N-PISEMA experiment which correlates (14)N quadrupolar coupling and (14)N-(1)H dipolar coupling. (14)N-PISEMA enables the use of (14)N quadrupolar coupling tensor as an ultra sensitive probe for peptide orientation and can be carried out without the need of isotope enrichment. The experiment is based on selective spin-exchange between a proton and a single-quantum transition of (14)N spins. The spin-exchange dynamics is described and the experiment is demonstrated with a natural abundant N-acetyl valine crystal sample.
authors.affiliation: Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA.
authors.forename: Chunqi
authors.initials: C
authors.lastname: Qian
authors.forename: Riqiang
authors.initials: R
authors.lastname: Fu
authors.forename: Peter
authors.initials: P
authors.lastname: Gor'kov
authors.forename: William W
authors.initials: WW
authors.lastname: Brey
authors.forename: Timothy A
authors.initials: TA
authors.lastname: Cross
authors.forename: Zhehong
authors.initials: Z
authors.lastname: Gan
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D009584:Nitrogen / Q000032:analysis / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins; D009584:Nitrogen