Prediction of Secondary Structure of Proteins. A Comparison of the ϕ,Ψ Angles Previously Predicted for Cytochrome c with Recent X-Ray Crystallographic Findings | Zendy

Elvin A. Kabat | Zendy; Tai Te Wu | Zendy

Open Access

Prediction 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

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.

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