title: Low-power high-resolution solid-state NMR of peptides and proteins.
abstract: We demonstrate that two-dimensional solid-state NMR chemical-shift correlation spectra can be recorded under low-power conditions. Except for the cross-polarization period, no rf-field amplitudes above 40 kHz are used. Such experiments require the use of fast (>50 kHz) magic-angle spinning (MAS). A comparison with the high-power version of the experiment shows no general line broadening but some changes in the polarization-transfer dynamics.
authors.affiliation: Physical Chemistry, ETH-Zürich, CH-8093 Zürich, Switzerland.
authors.forename: Matthias
authors.initials: M
authors.lastname: Ernst
authors.forename: Marcel A
authors.initials: MA
authors.lastname: Meier
authors.forename: Tiit
authors.initials: T
authors.lastname: Tuherm
authors.forename: Ago
authors.initials: A
authors.lastname: Samoson
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods*; D010456:Peptides, Cyclic / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
chemical_list: D010456:Peptides, Cyclic; D011506:Proteins; C100265:antamanide