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Hydrogen Bonding Modulates Binding of Exogenous Ligands in a Myoglobin Proximal Cavity Mutant
Alanine Amino Acid Substitution Animals Binding Sites Glycine Histidine Hydrogen Bonding Imidazoles Ligands Macromolecular Substances Metmyoglobin Models, Chemical Mutagenesis, Insertional Myoglobin Nitric Oxide Nuclear Magnetic Resonance,Biomolecular Protons Serine Threonine Whales
2016/5/23
In the sperm whale myoglobin mutant H93G, the proximal histidine is replaced by glycine, leaving a cavity in which exogenous imidazole can bind and ligate the heme iron (Barrick, D. (1994) Biochemistr...
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 ...