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Background: Protein structures incorporate characteristic three-dimensional elements defined by some or all of hydrogen bonding, dihedral angles and amino acid sequence. The software application, Structure Motivator, allows interactive exploration and analysis of such elements, and their resolution into sub-classes.
Results: Structure Motivator is a standalone application with an embedded relational database of proteins that, as a starting point, can furnish the user with a palette of unclassified small peptides or a choice of pre-classified structural motifs. Alternatively the application accepts files of data generated externally. After loading, the structural elements are displayed as two-dimensional plots of dihedral angles (φ/ψ, φ/χ1 or in combination) for each residue, with visualization options to allow the conformation or amino acid composition at one residue to be viewed in the context of that at other residues. Interactive selections may then be made and structural subsets saved to file for further sub-classification or external analysis. The application has been applied both to classical motifs, such as the β-turn, and ‘non-motif’ structural elements, such as specific segments of helices.
Conclusions: Structure Motivator allows structural biologists, whether or not they possess computational skills, to subject small structural elements in proteins to rapid interactive analysis that would otherwise require complex programming or database queries. Within a broad group of structural motifs, it facilitates the identification and separation of sub-classes with distinct stereochemical properties.
|Glasgow Author(s) Enlighten ID:||Leader, Dr David and Milner-White, Professor E|
|Authors:||Leader, D.P., and Milner-White, E.J.|
|College/School:||College of Medical Veterinary and Life Sciences > School of Life Sciences|
|Journal Name:||BMC Structural Biology|
|Publisher:||BioMed Central Ltd|
|Published Online:||01 January 2012|
|Copyright Holders:||Copyright © 2012 The Authors|
|First Published:||First published in BMC Structural Biology 12(1):26|
|Publisher Policy:||Reproduced under a Creative Commons License|