Introduction to rotational-echo, double-resonance NMR
نویسنده
چکیده
( ) ABSTRACT: Rotational-echo, double-resonance nuclear magnetic resonance REDOR is a magic-angle spinning experiment for measuring internuclear distances between heteronuclear spin pairs. The basic principles of the REDOR technique are presented. The experimental requirements necessary for quantitative REDOR measurements are also provided. Q 1998 John Wiley & Sons, Inc. Concepts Magn Reson 10: 277]289, 1998
منابع مشابه
Measurement of N–H bond lengths by rotational-echo double-resonance NMR spectroscopy
A method based on rotational-echo double-resonance (REDOR) NMR is proposed to measure H–N bond lengths under magic-angle-spinning. Protons are selectively polarized and evolve under the frequency-switched Lee– Goldburg (FSLG) homonuclear decoupling, while two N p pulses are applied to restore H–N dipolar interactions. Such a method relies on the H–N dipolar couplings and requires no knowledge o...
متن کاملHuman factor Xa bound amidine inhibitor conformation by double rotational-echo double resonance nuclear magnetic resonance and molecular dynamics simulations.
Double rotational-echo double resonance (double REDOR) NMR was used to investigate the conformation of a (13)C-, (15)N-, and (19)F-labeled inhibitor (Berlex Biosciences compound no. ZK-806299) bound to human factor Xa. Conformationally dependent carbon-fluorine dipolar couplings were measured by (13)C[(19)F] REDOR. Natural abundance carbon signals in the full-echo spectra were removed by (13)C[...
متن کاملX–H rotational-echo double-resonance NMR for torsion angle determination of peptides
C–H and N–H rotational-echo double-resonance (REDOR) NMR is developed for determining torsion angles in peptides. The distance between an X spin such as C or N and a proton is measured by evolving the proton magnetization under REDOR-recoupled X–H dipolar interaction. The proton of interest is selected through its directly bonded heteronuclear spin Y. The sidechain torsion angle v1 is extracted...
متن کاملConformational analysis of the Saccharomyces cerevisiae tridecapeptide mating pheromone by 13C,15N rotational-echo double resonance nuclear magnetic resonance spectroscopy.
The solid-state conformation of [Nle12]alpha-factor, the Saccharomyces cerevisiae tridecapeptide mating pheromone (WHWLQLKPGQPNleY), was investigated by 13C,15N rotational-echo double resonance (REDOR) nuclear magnetic resonance spectroscopy (NMR). Previous high-resolution NMR studies of [Nle12]alpha-factor in solution revealed a transient Type II beta-turn spanning residues 7-10 of the peptide...
متن کاملCharacterization of reactive sites in supported catalysts by 51V/15N rotational echo double resonance NMR spectroscopy: formation of phenylimido groups at surface-bound oxovanadium sites.
Silica-supported oxovanadium groups were reacted in a gas-solid reaction with aniline at 175 degrees C. The reaction was clean as monitored in situ by UV-vis spectroscopy and resulted in the elimination of water as the principal product of the reaction and the disappearance of the terminal V=O stretch in the Raman spectrum. 15N MAS solid-state NMR spectroscopy showed only a single nitrogen-cont...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 1998