Title : EPR characterization of the stereochemistry of the distal heme pocket of the engineered human myoglobin mutants.

Pub. Date : 1991 Dec 15

PMID : 1660880






3 Functional Relationships(s)
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1 Recombinant human myoglobin mutants with the distal histidine residue replaced by Leu, Val, or Gln residues have been prepared by site-directed mutagenesis and expression in Escherichia coli. Leucine myoglobin Homo sapiens
2 To our surprise, the distal Leu mutant has a less restricted, less sterically crowded distal heme pocket than that of the distal Val mutant myoglobin, despite the fact that Leu has a larger side chain volume than Val. Leucine myoglobin Homo sapiens
3 To our surprise, the distal Leu mutant has a less restricted, less sterically crowded distal heme pocket than that of the distal Val mutant myoglobin, despite the fact that Leu has a larger side chain volume than Val. Leucine myoglobin Homo sapiens