Improved resolution in 1H-detected 1H-15N correlation experiments.

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 Lett

journal_title

FEBS letters

authors

Norwood TJ,Boyd J,Campbell ID

doi

10.1016/0014-5793(89)81124-x

subject

Has Abstract

pub_date

1989-09-25 00:00:00

pages

369-71

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(89)81124-X

journal_volume

255

pub_type

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