Electrostatic effects in myoglobin. Application of the modified Tanford-Kirkwood theory to myoglobins from horse, California grey whale, harbor seal, and California sea lion.
The modified Tanford-Kirkwood electrostatic theory (Shire et al., 1974a) was applied to ferrimyoglobins from the following animal species: sperm whale (Physeter catodon), horse, California grey whale (Eschrichtius gibbosus), harbor seal (Phoca vitulina), and California sea lion (Zalophus californianus). Computations were made of the overall hydrogen ion titration curves of the proteins, and of pH and ionic strength variations of ionization equilibria for individual groups in the protein, with particular reference to the hemic acid ionization of the iron bound water molecule. Coordinates and static solvent accessibility were estimated in terms of the sperm whale myoglobin structure. Where possible, theoretical results and experimental data are compared. Some comparative features of charge and ionization properties among the various myoglobins are presented.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D010872:Caniformia; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009211:Myoglobin; D009994:Osmolar Concentration; D046070:Sea Lions; D013045:Species Specificity; D014907:Whales
D000596:Amino Acids; D009211:Myoglobin