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

DOI10.1016/J.JTBI.2011.06.011zbMATH Open1397.92537OpenAlexW1999277606WikidataQ84453802 ScholiaQ84453802MaRDI QIDQ1786069FDOQ1786069

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

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

zbMATH Keywords

beta strandextended loopsequence and structure

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20)

Cites Work

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

This page was built for publication: Conformation and sequence evidence for two-fold symmetry in left-handed beta-helix fold

Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q1786069)