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

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

Related Articles NMR studies of the solution properties of recombinant murine interleukin-6.

Biochim Biophys Acta. 1995 Jun 12;1249(2):189-203

Authors: Morton CJ, Bai H, Zhang JG, Hammacher A, Norton RS, Simpson RJ, Mabbutt BC

The effects of solvent, pH and temperature on the 1H-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 pKa 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. 1H and 15N resonances of residues Thr-4 to Val-21 are assigned from three-dimensional 1H-15N 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.

PMID: 7599173 [PubMed - indexed for MEDLINE]



Source: PubMed
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