| Literature DB >> 2966074 |
A M Gronenborn1, P T Wingfield, H R McDonald, U Schmeissner, G M Clore.
Abstract
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.Entities:
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Year: 1988 PMID: 2966074 DOI: 10.1016/0014-5793(88)80717-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124