Analysis of protein crystallographic structural data: analysis of the orientation of peptide planes |
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Authors: | R. Srinivasan V. Ravichandran |
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Affiliation: | Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Madras-600 025, India |
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Abstract: | A new dihedral angle parameter θ′, defined by Ci?1|Ni…Ci|Ni+1, involving pairs of backbone atoms in two adjacent peptide planes is used in this paper to analyse the relative orientation of the peptide planes in a protein chain. The equiangle contours for this parameter on the ?+ψ in an approximately linear way. Thus, θ′ serves as a good single parameter representation for chainfolding characterization by bringing out the relative orientation of successive peptide planes. Unlike the earlier proposed θ which gives the gross folding features, θ′ can be applied for nonregular helical features. Its utility in the detection of bend regions in protein chains is compared with that of θ through theoretically calculated tables as well as examples from actual proteins. |
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Keywords: | Proteins protein structure peptide plane orientations folding characterization |
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