Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state-Reference-Cited by-同舟云学术

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Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state

Published:2003-01 Issue:1 Volume:160 Page:1-12
ISSN:1090-7807
Container-title:Journal of Magnetic Resonance
language:en
Short-container-title:Journal of Magnetic Resonance

Author:

Petkova Aneta T,Baldus Marc,Belenky Marina,Hong Mei,Griffin Robert G,Herzfeld Judith

Publisher

Elsevier BV

Subject

Condensed Matter Physics,Nuclear and High Energy Physics,Biochemistry,Biophysics

Reference44 articles.

1. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin;Ikura;Biochemistry,1990

2. Nuclear magnetic resonance spectra from a crystal rotated at high speed;Andrew;Nature,1958

3. Free induction decays of rotating solids;Lowe;Phys. Rev. Lett.,1959

4. Two-dimensional 13C NMR of highly oriented polyethylene;Opella;J. Chem. Phys.,1977

5. Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules;Sanders;Progr. NMR Spectrosc.,1994

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1. Sample Preparation and Technical Setup for NMR Spectroscopy with Integral Membrane Proteins;Methods in Molecular Biology;2020

2. Proton-Assisted Recoupling (PAR) in Peptides and Proteins;The Journal of Physical Chemistry B;2017-11-27

3. 3D MAS NMR Experiment Utilizing Through-Space 15N–15N Correlations;Journal of the American Chemical Society;2017-05-03

4. Spin-locking and cross-polarization under magic-angle spinning of uniformly labeled solids;Journal of Magnetic Resonance;2015-07

5. On the problem of resonance assignments in solid state NMR of uniformly 15N,13C-labeled proteins;Journal of Magnetic Resonance;2015-04

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