| First Author | Morton CJ | Year | 1995 |
| Journal | Biochim Biophys Acta | Volume | 1249 |
| Issue | 2 | Pages | 189-203 |
| PubMed ID | 7599173 | Mgi Jnum | J:26179 |
| Mgi Id | MGI:73844 | Doi | 10.1016/0167-4838(95)00023-n |
| Citation | Morton CJ, et al. (1995) NMR studies of the solution properties of recombinant murine interleukin-6. Biochim Biophys Acta 1249(2):189-203 |
| abstractText | 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. |
