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NMR-STUDIES OF THE SOLUTION PROPERTIES OF RECOMBINANT MURINE INTERLEUKIN-6


Morton, CJ; BAI, HP; Zhang, JG; Hammacher, A; Norton, RS; Simpson, RJ; MABBUTT, BC
1995-06-12
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Journal Article
1249
2
189-203
The effects of solvent, pH and temperature on the H-1-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 pK(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. H-1 and N-15 resonances of residues Thr-4 to Val-21 are assigned from three-dimensional H-1-N-15 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.
ELSEVIER SCIENCE BV
NUCLEAR-MAGNETIC-RESONANCE; COLONY-STIMULATING FACTOR; TIME-DOMAIN DATA; SOLVENT SUPPRESSION; BIOLOGICAL-ACTIVITY; HISTIDINE-RESIDUES; FOURIER-TRANSFORM; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; H-1-NMR SPECTRA
10.1016/0167-4838(95)00023-N
Refer to copyright notice on published article.

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Creation Date 1995-06-12 12:00:00