Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure
DOI10.3390/SYM4010015zbMATH Open1352.92114OpenAlexW2124109894MaRDI QIDQ350577FDOQ350577
Authors: Jaime Nava, Vladik Kreinovich 
Publication date: 9 December 2016
Published in: Symmetry (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.3390/sym4010015
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Cited In (8)
- Determination of helix orientations in proteins
- Symmetry of helicoidal biopolymers in the frameworks of algebraic geometry: \(\alpha\)-helix and DNA structures
- Conformation and sequence evidence for two-fold symmetry in left-handed beta-helix fold
- Hidden symmetries in the primary sequences of beta-barrel family
- A comment on the protein folds as platonic forms
- Parabolic section and distance excess of space curves applied to protein structure classification
- Crystals, proteins, stability and isoperimetry
- Title not available (Why is that?)
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