Prediction of secondary structure of proteins. A comparison of the phi, psi angles previously predicted for cytochrome c with recent x-ray crystallographic findings.
Newer data from the x-ray crystallographic studies of tuna heart ferrocytochrome c have increased the number of residues in alpha-helical segments. This provided an objective test of our method of predicting varphi,Psi values for cytochrome c using the sequences of 18 cytochromes c and twenty 20 x 20 tables for the varphi,Psi values of tripeptides in 10 other proteins whose three-dimensional structures were known from x-ray crystallographic studies. Of the 32 residues now considered from x-ray data to be in alpha-helices, 27 had been predicted to be in the alpha-helical domain.
D000818:Animals; D003574:Cytochrome c Group; D005399:Fishes; D009206:Myocardium / Q000032:analysis; D011487:Protein Conformation; D014961:X-Ray Diffraction
D003574:Cytochrome c Group