On the difference in stability between horse and sperm whale myoglobins.
The work in the literature on apomyoglobin is almost equally divided between horse and sperm whale myoglobins. The two proteins share high homology, show similar folding behavior, and it is often assumed that all folding phenomena found with one protein will also be found with the other. We report data at equilibrium showing that horse myoglobin was 2.1 kcal/mol less stable than sperm whale myoglobin at pH 5.0, and aggregated at high concentrations as measured by gel filtration and analytical ultracentrifugation experiments. The higher stability of sperm whale myoglobin was identified for both apo and holo forms, and was independent of pH from 5 to 8 and of the presence of sodium chloride. We also show that the substitution of sperm whale myoglobin residues Ala15 and Ala74 to Gly, the residues found at positions 15 and 74 in horse myoglobin, decreased the stability by 1.0 kcal/mol, indicating that helix propensity is an important component of the explanation for the difference in stability between the two proteins.
Regis
Wiliam C B
WC
Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, P.O. Box 6192, ZIP Code 13084971, Campinas SP, Brazil.
Fattori
Juliana
J
Santoro
Marcelo M
MM
Jamin
Marc
M
Ramos
Carlos H I
CH
D000818:Animals; D001483:Base Sequence; D002850:Chromatography, Gel; D004305:Dose-Response Relationship, Drug; D006736:Horses; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D013045:Species Specificity; D013696:Temperature; D014461:Ultracentrifugation; D014508:Urea / Q000494:pharmacology; D014907:Whales
D009211:Myoglobin; D014508:Urea