Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution
- National Institutes of Health, Bethesda, MD (USA)
A method is presented that dramatically improves the resolution of protein nuclear magnetic resonance (NMR) spectra by increasing their dimensionality to four. The power of this technique is demonstrated by the application of four-dimensional carbon-13 - nitrogen-15 ({sup 13}C-{sup 15}N) - edited nuclear Overhauser effect (NOE) spectroscopy to interleukin-1{beta}, a protein of 153 residues. The NOEs between NH and aliphatic protons are first spread out into a third dimension by the {sup 15}N chemical shift of the amide {sup 15}N atom and subsequently into a fourth dimension by the {sup 13}C chemical shift of the direct bonded {sup 13}C atoms. By this means ambiguities in the assignment of NOEs between NH and aliphatic protons that are still present in the three-dimensional {sup 15}N-edited NOE spectrum due to extensive chemical shift overlap and degeneracy of aliphatic resonances are completely removed. Consequently, many more approximate interproton distance restraints can be obtained from the NOE data than was heretofore possible, thereby expanding the horizons of three-dimensional structure determination by NMR to larger proteins.
- OSTI ID:
- 6367982
- Journal Information:
- Science (Washington, D.C.); (USA), Vol. 249:4967; ISSN 0036-8075
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
LYMPHOKINES
MOLECULAR STRUCTURE
CARBON 13
CHEMICAL SHIFT
NITROGEN 15
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
OVERHAUSER EFFECT
PROTONS
RESOLUTION
TRACER TECHNIQUES
BARYONS
CARBON ISOTOPES
ELEMENTARY PARTICLES
EVEN-ODD NUCLEI
FERMIONS
GROWTH FACTORS
HADRONS
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MITOGENS
NITROGEN ISOTOPES
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PROTEINS
RESONANCE
SPECTRA
STABLE ISOTOPES
550201* - Biochemistry- Tracer Techniques