Analysis of protein crystallographic structural data: analysis of the orientation of peptide planes

Srinivasan, R. ; Ravichandran, V. (1982) Analysis of protein crystallographic structural data: analysis of the orientation of peptide planes International Journal of Biological Macromolecules, 4 (4). pp. 211-214. ISSN 0141-8130

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/014181...

Related URL: http://dx.doi.org/10.1016/0141-8130(82)90017-4

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 Φ+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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Proteins; Protein Structure; Peptide Plane Orientations; Folding Characterization
ID Code:36589
Deposited On:12 Apr 2011 10:23
Last Modified:12 Apr 2011 10:23

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