Article
A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket.
Biochimica et biophysica acta - 15 Aug 1997
Maurus R, Overall C M, Bogumil R, Luo Y, Mauk A G, Smith M, Brayer G D
Abstract excerpt
Well-ordered internal amino acids can contribute significantly to the stability of proteins. To investigate the importance of the hydrophobic packing interface between helices G and H in the proximal heme pocket of horse heart myoglobin, the highly conserved amino acid, Leu104, was substituted with asparagine, a polar amino acid of similar size. The Leu104Asn mutant protein and its recombinant wild-type horse...
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