PlumX Metrics
Embed PlumX Metrics

NMR studies of the solution properties of recombinant murine interleukin-6

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, ISSN: 0167-4838, Vol: 1249, Issue: 2, Page: 189-203
1995
  • 8
    Citations
  • 0
    Usage
  • 2
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

Article Description

The effects of solvent, pH and temperature on the 1 H-NMR spectra of recombinant murine interleukin-6 (IL-6) are described. Assignments made from two-dimensional homonuclear spectra are presented for resonances of the fifteen aromatic amino-acid side chains. A time-dependent loss of intensity was observed for all resonances in the spectrum of IL-6, probably as a result of aggregation. This aggregation is markedly temperature-dependent. The p K a values of the four histidine residues in murine IL-6 has been measured; one has a value of 5.5, approx. one pH unit less than the value exhibited by the other three. Analysis of the NOESY spectra has allowed a preliminary characterisation of the nature of interactions among the aromatic side chains within the protein fold. 1 H and 15 N resonances of residues Thr-4 to Val-21 are assigned from three-dimensional 1 H- 15 N correlated spectroscopy, and evidence is presented for these residues comprising a mobile N-terminal tail with little ordered structure. An N-terminal mutant lacking the first 22 residues of the murine IL-6 sequence and known to possess full biological activity was also examined and shown to have essentially retained the tertiary fold of the native molecule.

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know