ArticlePloS one2020
Side chain flexibility and the symmetry of protein homodimers.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Molecular Characterization of Publicly Available NDV F Gene Sequences From Bangladesh (2010-2024).Veterinary medicine international · 2026Article
- Continuous symmetry and chirality measures: approximate algorithms for large molecular structures.Journal of cheminformatics · 2023Article
- From Chaos to Ordering: New Studies in the Shannon Entropy of 2D Patterns.Entropy (Basel, Switzerland) · 2022Review
- Structure of the Acinetobacter baumannii PmrA receiver domain and insights into clinical mutants affecting DNA binding and promoting colistin resistance.Journal of biochemistry · 2022Article
- Functional Characterization of 21 Rare AllelicJournal of personalized medicine · 2021Article
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Authors and funding
2 authors.
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Abstract
A comprehensive analysis of crystallographic data of 565 high-resolution protein homodimers comprised of over 250,000 residues suggests that amino acids form two groups that differ in their tendency to distort or symmetrize the structure of protein homodimers. Residues of the first group tend to distort the protein homodimer and generally have long or polar side chains. These include: Lys, Gln, Glu, Arg, Asn, Met, Ser, Thr and Asp. Residues of the second group contribute to protein symmetry and are generally characterized by short or aromatic side chains. These include: Ile, Pro, His, Val, Cys, Leu, Trp, Tyr, Phe, Ala and Gly. The distributions of the continuous symmetry measures of the proteins and the continuous chirality measures of their building blocks highlight the role of side chain geometry and the interplay between entropy and symmetry in dictating the conformational flexibility of proteins.
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