Journal article

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

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

Biochimica Et Biophysica Acta Bba Protein Structure and Molecular | ELSEVIER SCIENCE BV | Published : 1995

Abstract

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 ..

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University of Melbourne Researchers