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Title: Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution

Abstract

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.

Authors:
; ; ;  [1]
  1. National Institutes of Health, Bethesda, MD (USA)
Publication Date:
OSTI Identifier:
6367982
Resource Type:
Journal Article
Journal Name:
Science (Washington, D.C.); (USA)
Additional Journal Information:
Journal Volume: 249:4967; Journal ID: ISSN 0036-8075
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 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

Citation Formats

Kay, L E, Clore, G M, Bax, A, and Gronenborn, A M. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution. United States: N. p., 1990. Web. doi:10.1126/science.2377896.
Kay, L E, Clore, G M, Bax, A, & Gronenborn, A M. Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution. United States. https://doi.org/10.1126/science.2377896
Kay, L E, Clore, G M, Bax, A, and Gronenborn, A M. 1990. "Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution". United States. https://doi.org/10.1126/science.2377896.
@article{osti_6367982,
title = {Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1. beta. in solution},
author = {Kay, L E and Clore, G M and Bax, A and Gronenborn, A M},
abstractNote = {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.},
doi = {10.1126/science.2377896},
url = {https://www.osti.gov/biblio/6367982}, journal = {Science (Washington, D.C.); (USA)},
issn = {0036-8075},
number = ,
volume = 249:4967,
place = {United States},
year = {Fri Jul 27 00:00:00 EDT 1990},
month = {Fri Jul 27 00:00:00 EDT 1990}
}