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Improved resolution in 1 H‐detected 1 H‐ 15 N correlation experiments
Author(s) -
Norwood T.J.,
Boyd J.,
Campbell I.D.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81124-x
Subject(s) - heteronuclear molecule , resolution (logic) , coherence (philosophical gambling strategy) , spectral line , physics , quantum correlation , quantum , chemistry , atomic physics , nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , quantum mechanics , quantum dynamics , quantum discord , artificial intelligence , computer science
The determination of protein structure by NMR is restricted at molecular masses above 10 kDa by overlapping resonances. One way of overcoming this problem is to label the protein with 15 N. The conventional way to record 15 N spectra is to use heteronuclear multiple‐quantum coherence. We present here an alternative approach based on 15 N single‐quantum coherence. This is shown to have substantial advantages over the multiple‐quantum method, including better F 1 resolution.