hNCOcanH pulse sequence and a robust protocol for rapid and unambiguous assignment of backbone (1 HN , 15 N and 13 C′) resonances in 15 N/13 C-labeled proteins-Reference-Cited by-同舟云学术

hNCOcanH pulse sequence and a robust protocol for rapid and unambiguous assignment of backbone (1 HN , 15 N and 13 C′) resonances in 15 N/13 C-labeled proteins

Published:2011-08-05 Issue:9 Volume:49 Page:575-583
ISSN:0749-1581
Container-title:Magnetic Resonance in Chemistry
language:en
Short-container-title:Magn. Reson. Chem.

Author:

Kumar Dinesh,Hosur Ramakrishna V.

Publisher

Wiley

Subject

General Materials Science,General Chemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/mrc.2787/fullpdf

Reference41 articles.

1. An Efficient High-Throughput Resonance Assignment Procedure for Structural Genomics and Protein Folding Research by NMR

2. A novel protocol based on HN(C)N for rapid resonance assignment in (15N, 13C) labeled proteins: implications to structural genomics

3. 3D Triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins

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1. Longitudinal relaxation properties of 1HN and 1Hα determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs);Journal of Magnetic Resonance;2015-05

2. NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines;Advances in Experimental Medicine and Biology;2015

3. Pseudo 5D HN(C)N experiment to facilitate the assignment of backbone resonances in proteins exhibiting high backbone shift degeneracy;Chemical Physics;2014-09

4. New 13C-detected experiments for the assignment of intrinsically disordered proteins;Journal of Biomolecular NMR;2014-04-04

5. Practical aspects of NMR signal assignment in larger and challenging proteins;Progress in Nuclear Magnetic Resonance Spectroscopy;2014-04