{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo L"],"funding":["NCRR NIH HHS"],"pagination":["7868-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2904518"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["132(23)"],"pubmed_abstract":["We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O...H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallographic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone."],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues."],"pmcid":["PMC2904518"],"funding_grant_id":["S10 RR013866-01"],"pubmed_authors":["Zhang W","Guo L","Reidenbach AG","Choi SH","Guzei IA","Almeida AM","Gellman SH"],"additional_accession":[]},"is_claimable":false,"name":"Helix formation in preorganized beta/gamma-peptide foldamers: hydrogen-bond analogy to the alpha-helix without alpha-amino acid residues.","description":"We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O...H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallographic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone.","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jun","modification":"2025-04-04T11:31:28.516Z","creation":"2019-03-26T23:28:39Z"},"accession":"S-EPMC2904518","cross_references":{"pubmed":["20491510"],"doi":["10.1021/ja103233a"]}}