Open AccessPrediction of Secondary Structure of Proteins. A Comparison of the ϕ,Ψ Angles Previously Predicted for Cytochrome c with Recent X-Ray Crystallographic Findings
Author(s) -
Elvin A. Kabat,
Tai Te Wu
Publication year - 1974
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.3.899
Subject(s) - crystallography , cytochrome c , protein structure , chemistry , x ray , physics , biochemistry , mitochondrion , quantum mechanics
Newer data from the x-ray crystallographic studies of tuna heart ferrocytochromec have increased the number of residues in α-helical segments. This provided an objective test of our method of predicting ϕ,Ψ values for cytochromec using the sequences of 18 cytochromesc and twenty 20 × 20 tables for the ϕ,Ψ 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 α-helices, 27 had been predicted to be in the α-helical domain.