A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C′ chemical shifts in 15N13C-labelled proteins
Author:
Publisher
Elsevier BV
Subject
General Engineering
Reference27 articles.
1. Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins. 2. Combined Use of Correlated Spectroscopy and Nuclear Overhauser Spectroscopy for Sequential Assignments of Backbone Resonances and Elucidation of Polypeptide Secondary Structures
2. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra
3. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra
4. NMR of Proteins and Nucleic Acids;Wüthrich,1986
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