Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples.

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Abstract Text:

Alexander A Nevzorov,Stanley J Opella,

Solid-state NMR experiments benefit from being performed at high fields, and this is essential in order to obtain spectra with the resolution and sensitivity required for applications to protein structure determination in aligned samples. Since the amount of rf power that can be applied is limited, especially for aqueous protein samples, the most important pulse sequences suffer from bandwidth limitations resulting from the same spread in chemical shift frequencies that aids resolution. SAMPI4 is a pulse sequence that addresses these limitations. It yields separated local field spectra with narrower and more uniform linewidths over the entire spectrum than the currently used PISEMA and SAMMY experiments. In addition, it is much easier to set up on commercial spectrometers and can be incorporated as a building block into other multidimensional pulse sequences. This is illustrated with a two-dimensional HETCOR experiment, where it is crucial to transfer polarization from the amide protons to their directly bonded nitrogens over a wide range of chemical shift frequencies. A quantum-mechanical treatment of the spin Hamiltonians under high-power rf pulses is presented which gives the scaling factor for SAMPI4 as well as the durations of the rf pulses to achieve optimal decoupling.

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Publishing Authors By Initials

AA Nevzorov,SJ Opella,

For similar information science: computing methodologies: signal processing, computer-assisted research abstracts see: information science: computing methodologies: signal processing, computer-assisted research

PUBMED ID PMID:

MEDLINE DATE:

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of magnetic resonance (San Diego, Calif. :

VOLUME: 185

Page Numbers: 59-70

Journal Abbreviation: J. Magn. Reson.

ISSN: 1090-7807

DAY: 30

MONTH: 10

YEAR: 2006

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9707935

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Keywords Mesh Terms:

KEYWORDS: Signal Processing, Computer-Assisted

MESH TERMS: chemistry

Chemical & Substance for Abstract: Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples. Information

Substance Name: Protons

Registry Number: 0

Grant and Affiliation Information for Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples.

AFFILIATION: Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0307, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01GM066978

ACRONYM: GM

MEDLINETA: J Magn Reson

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples Related Publications

• An efficient (1)H/(31)P double-resonance solid-state NMR probe that utilizes a scroll coil.
• Assigning solid-state NMR spectra of aligned proteins using isotropic chemical shifts.
• Bicelle samples for solid-state NMR of membrane proteins.
• Dipolar waves as NMR maps of protein structure.
• High-resolution NMR spectroscopy of a GPCR in aligned bicelles.
• NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization.
• Proton-detected separated local field spectroscopy.
• Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples.
• Shiftless nuclear magnetic resonance spectroscopy.
• Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field.
• Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy.
• Three-dimensional experiment for solid-state NMR of aligned protein samples in high field magnets.
• Triple resonance experiments for aligned sample solid-state NMR of (13)C and (15)N labeled proteins.