Predicted secondary structure of horse muscle acylphosphatase. Comparison with circular dichroism measurements.
We have predicted the secondary structure of horse muscle acylphosphatase by the statistical method of Chou and Fasman. In addition, we have studied the circular dichroism spectra of the enzyme, obtaining values for comparison to the predicted results. Discrepancies were found for the alpha-helix content estimated by the two methods.
D017766:Acid Anhydride Hydrolases; D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D006736:Horses; D009132:Muscles / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases; D011487:Protein Conformation; D013223:Statistics as Topic; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase