Homonuclear Hartmann-Hahn transfer with reduced relaxation losses by use of the MOCCA-XY16 multiple pulse sequence.
Homonuclear Hartmann-Hahn transfer is one of the most important building blocks in modern high-resolution NMR. It constitutes a very efficient transfer element for the assignment of proteins, nucleic acids, and oligosaccharides. Nevertheless, in macromolecules exceeding approximately 10 kDa TOCSY-experiments can show decreasing sensitivity due to fast transverse relaxation processes that are active during the mixing periods. In this article we propose the MOCCA-XY16 multiple pulse sequence, originally developed for efficient TOCSY transfer through residual dipolar couplings, as a homonuclear Hartmann-Hahn sequence with improved relaxation properties. A theoretical analysis of the coherence transfer via scalar couplings and its relaxation behavior as well as experimental transfer curves for MOCCA-XY16 relative to the well-characterized DIPSI-2 multiple pulse sequence are given.
Furrer
Julien
J
Institut für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany.
Kramer
Frank
F
Marino
John P
JP
Glaser
Steffen J
SJ
Luy
Burkhard
B
D000465:Algorithms; D000818:Animals; D016477:Artifacts; D002645:Chickens; D004527:Egg Proteins / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D009842:Oligopeptides / Q000737:chemistry*; D012313:RNA / Q000737:chemistry*; D012542:Scattering, Radiation; D012815:Signal Processing, Computer-Assisted; D013113:Spin Labels
D004527:Egg Proteins; D009842:Oligopeptides; D013113:Spin Labels; D012313:RNA; D009113:Muramidase