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Site directed mutants of human interleukin-1 alpha: a 1H-NMR and receptor binding study.

Mutant human interleukin-1 alpha proteins were constructed by oligonucleotide directed mutagenesis. Six different mutants were tested for receptor binding activity and showed no alteration with respect to the wild-type protein. Analysis of these mutants by nuclear magnetic resonance spectroscopy confirmed the structural integrity of the mutant proteins and permitted the sequence specific assignment of the histidine and tryptophan residues.