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Site directed mutants of human interleukin‐1α: A 1 H‐NMR and receptor binding study
Author(s) -
Gronenborn Angela M.,
Wingfield Paul T.,
McDonald H.Robson,
Schmeissner Ursula,
Clore G.Marius
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80717-8
Subject(s) - mutant , site directed mutagenesis , histidine , mutagenesis , chemistry , nuclear magnetic resonance spectroscopy , tryptophan , binding site , microbiology and biotechnology , biochemistry , biology , stereochemistry , gene , amino acid
Mutant human interleukin‐1α 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.