Characterization and comparison of protein structures. Part II-comparison.
The Fourier methods are applied to the pairwise comparison of Calpha-backbones in protein structures. The technique allows to assess both the general similarity and the main origins of resemblance (coincident periodicities, similarity of fragments, or large-scale semblance of folding). The analogous methods can be extended to the study of correlations between the structural characteristics for the Calpha-backbone of one protein and the distribution of physico-chemical parameters along the primary amino acid sequence for the other. Finally, we discuss the problem of clusterization of pairwise data into tree-like hierarchical system.
Chechetkin
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VR
Theoretical Department of Division for Perspective Investigations, Troitsk Institute of Innovation and Thermonuclear Investigations (TRINITI), Moscow Region, 142092 Troitsk, Russia. ezhov@fly.triniti.troitsk.ru
Lobzin
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VV
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000502:physiology; D000818:Animals; D005583:Fourier Analysis; D008956:Models, Chemical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000502:physiology
D000596:Amino Acids; D011506:Proteins