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Perturbations of the Distal Heme Pocket in Human Myoglobin Mutants Probed by Infrared Spectroscopy of Bound CO:Correlation with Ligand Binding Kinetics
Distal Heme Pocket Human Myoglobin Mutants Probed Infrared Spectroscopy Bound CO:Correlation Ligand Binding Kinetics
2016/5/23
The infrared spectra of CO bound to human myoglobin and myoglobin mutants at positions His-64, Val-68, Asp-60, and Lys-45 on the distal side have been measured between 100 and 300 K. Large differences...
CO Recombination to Human Myoglobin Mutants in Glycerol-Water Solutions
CO Recombination Human Myoglobin Mutants Glycerol-Water Solutions
2016/5/23
The kinetics of CO recombination to site-specific mutants of human myoglobin have been studied by flash photolysis in the temperature range 250-320 K on the nanosecond to second time scale in 75% glyc...
Ligand and Proton Exchange Dynamics in Recombinant Human Myoglobin Mutants
Mb myoglobin n.m.r. nuclear magnetic resonance fwhm full width at half maximum TSP sodium 3-trimethyl silyl propionate DSS 4,4-dimethyl-4-sila pentane-1-sulfonate
2016/5/20
Site-specific mutants of human myoglobin have been prepared in which lysine 45 is replaced by arginine (K45R) and aspartate 60 by glutamate (D60E), in order to examine the influence of these residues ...