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Analysis of Cα geometry in protein structures
Author(s) -
Oldfield T. J.,
Hubbard R. E.
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340180404
Subject(s) - ramachandran plot , dihedral angle , geometry , crystallography , protein structure , basis (linear algebra) , chemistry , resolution (logic) , biomolecular structure , molecule , mathematics , computer science , artificial intelligence , hydrogen bond , organic chemistry , biochemistry
The polypeptide of a protein molecule can be considered as a chain of Cα atoms linked by pseudobonds between the Cα atoms of successive amino acid residues. This paper presents an analysis of the angle and dihedral angles made by these pseudobonds in protein structures determined at high resolution by X‐ray crystallography. This analysis reveals a strong correlation between Cα geometry and the protein fold. The regular features of protein secondary structure such as α‐helix and α‐sheet are very clearly defined. In addition, it is possible to identify with some confidence the discrete populations of particular conformations of α‐turn. Comparison with the traditional Ramachandran type of plot demonstrates that an analysis of protein structure on the basis of Cα geometry provides a richer description of protein conformation. In addition, the characteristics of this geometry could be a useful guide in model building of protein structure. © 1994 John Wiley & Sons, Inc.