{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Martinez-Parra JM"],"funding":["European Research Council"],"pagination":["6987"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11325010"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["The structure of helical polymers is dictated by the molecular chirality of their monomer units. Particularly, macromolecular helices with monomer sequence control have the potential to generate chiral topologies. In α-helical folded peptides, the sequential repetition of amino acids generates a chiral layer defined by the amino acid side chains projected outside the amide backbone. Despite being closely related to peptides' structural and functional properties, to the best of our knowledge, a general exo-helical symmetry model has not been yet described for the α-helix. Here, we perform the theoretical, computational, and spectroscopic elucidation of the α-helix principal exo-helical topologies. Non-canonical labeled amino acids are employed to spectroscopically characterize the different"],"journal":["Nature communications"],"pubmed_title":["Exo-chirality of the α-helix."],"pmcid":["PMC11325010"],"funding_grant_id":["677786","838002"],"pubmed_authors":["Gomez-Ojea R","Calvelo M","Daudey GA","Bergueiro J","Martinez-Parra JM","Montenegro J","Fernandez-Caro H"],"additional_accession":[]},"is_claimable":false,"name":"Exo-chirality of the α-helix.","description":"The structure of helical polymers is dictated by the molecular chirality of their monomer units. Particularly, macromolecular helices with monomer sequence control have the potential to generate chiral topologies. In α-helical folded peptides, the sequential repetition of amino acids generates a chiral layer defined by the amino acid side chains projected outside the amide backbone. Despite being closely related to peptides' structural and functional properties, to the best of our knowledge, a general exo-helical symmetry model has not been yet described for the α-helix. Here, we perform the theoretical, computational, and spectroscopic elucidation of the α-helix principal exo-helical topologies. Non-canonical labeled amino acids are employed to spectroscopically characterize the different","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2025-04-19T14:50:23.571Z","creation":"2025-04-19T14:50:23.571Z"},"accession":"S-EPMC11325010","cross_references":{"pubmed":["39143054"],"doi":["10.1038/s41467-024-51072-8"]}}