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
- 8Citations
- 2Captures
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef6
- Captures2
- Readers2
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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/016748389500023N; http://dx.doi.org/10.1016/0167-4838(95)00023-n; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029004129&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/7599173; http://linkinghub.elsevier.com/retrieve/pii/016748389500023N; http://api.elsevier.com/content/article/PII:016748389500023N?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:016748389500023N?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/016748389500023N; http://dx.doi.org/10.1016/0167-4838%2895%2900023-n; https://dx.doi.org/10.1016/0167-4838%2895%2900023-n
Elsevier BV
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