ArticlePhilosophical transactions. Series A, Mathematical, physical, and engineering sciences2014
How does symmetry impact the flexibility of proteins?
Article in Philosophical transactions. Series A, Mathematical, physical, and engineering sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Article
- TRAMbio: a flexible python package for graph rigidity analysis of macromolecules.BMC bioinformatics · 2025Article
- Article
- Improved algorithms for quantifying the near symmetry of proteins: complete side chains analysis.Journal of cheminformatics · 2019Article
- Universal folding pathways of polyhedron nets.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Geometric analysis characterizes molecular rigidity in generic and non-generic protein configurations.Journal of the mechanics and physics of solids · 2015Article
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3 authors.
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Abstract
It is well known that (i) the flexibility and rigidity of proteins are central to their function, (ii) a number of oligomers with several copies of individual protein chains assemble with symmetry in the native state and (iii) added symmetry sometimes leads to added flexibility in structures. We observe that the most common symmetry classes of protein oligomers are also the symmetry classes that lead to increased flexibility in certain three-dimensional structures-and investigate the possible significance of this coincidence. This builds on the well-developed theory of generic rigidity of body-bar frameworks, which permits an analysis of the rigidity and flexibility of molecular structures such as proteins via fast combinatorial algorithms. In particular, we outline some very simple counting rules and possible algorithmic extensions that allow us to predict continuous symmetry-preserving motions in body-bar frameworks that possess non-trivial point-group symmetry. For simplicity, we focus on dimers, which typically assemble with twofold rotational axes, and often have allosteric function that requires motions to link distant sites on the two protein chains.
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