Published February 15, 1989
| Version v1
Journal article
Three-dimensional heteronuclear NMR of 15N-labeled proteins
- 1. National Institutes of Health, Bethesda, MD (USA)
Description
The use of a 3D NMR technique has been shown to remove the problems of degenerate chemical shifts. A very sensitive 3D experiment for unraveling the regular protein NOESY spectrum is reported here. The method involves the 15N labelling of the protein and is described in some detail. The sensitivity of this heteronuclear 3D technique is excellent, and resonance overlap in the S. Nase 3D spectrum is minimal, despite the relatively coarse digitization. 14 references, 2 figures
Additional details
Publishing Information
- Journal Title
- Journal of the American Chemical Society
- Journal Volume
- 111
- Journal Issue
- 4
- Series
- J. Am. Chem. Soc.
- Journal Page Range
- 1515-1517
- ISSN
- 0002-7863
- CODEN
- JACSA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 21035817
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- LABELLED COMPOUNDS; MOLECULAR STRUCTURE; NITROGEN 15; NUCLEAR MAGNETIC RESONANCE; PROTEINS; TRACER TECHNIQUES
- Descriptors DEC
- ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; NITROGEN ISOTOPES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; RESONANCE; STABLE ISOTOPES