Abstract:
: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 15N. The conventional way to record 15N spectra is to use heteronuclear multiple-quantum coherence. We present here an alternative approach based on 15N single-quantum coherence. This is shown to have substantial advantages over the multiple-quantum method, including better F1 resolution.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Norwood TJ,Boyd J,Campbell IDdoi
10.1016/0014-5793(89)81124-xsubject
Has Abstractpub_date
1989-09-25 00:00:00pages
369-71issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(89)81124-Xjournal_volume
255pub_type
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