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The three-dimensional structure of sperm whale myoglobin His 64 (E7)->Val,Thr 64 (E10)->Arg double mutant has been studied by X-ray crystallography at 1.6 Å resolution, and refined to a crystallographic R-factor of 0.197. The Arg 67 (E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 Å from...
Equilibrium and kinetic experiments on site-directed mutants of a synthetic sperm whale myoglobin (Mb) gene have been performed. Results on the reactivity on both ferric and ferrous wild type and mutants Mb's are presented. Analysis of ligand binding to His(E7) Val and His(E7) Val-Thr(E10) Arg mutants compared to wild-type sperm whale, horse and Aplysia limaelna Mb's, shows that the introduction of...
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