Conformation and sequence evidence for two-fold symmetry in left-handed beta-helix fold

DOI10.1016/J.JTBI.2011.06.011MaRDI QIDQ1786069zbMATH OpenOpenAlexWikidataFDO

Authors Xiaojuan Shen

Publication date 24 September 2018

Published in Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1016/j.jtbi.2011.06.011

zbMATH Keywords

beta strandextended loopsequence and structure

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20)

Recommendations

• Research in Computational Molecular Biology
• Helix-helix interactions and their impact on protein motifs and assemblies
• Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure
• Helical assemblies: structure determinants
• Studies on the rules of \(\beta\)-strand alignment in a protein \(\beta\)-sheet structure

Cites work

• A common sequence-associated physicochemical feature for proteins of beta-trefoil family
• A simple method of identifying symmetric substructures of proteins
• Nonlinear analysis of sequence symmetry of beta-trefoil family proteins

Cited in

(2)

• Research in Computational Molecular Biology
• A common sequence-associated physicochemical feature for proteins of beta-trefoil family

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