{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu X"],"funding":["NSF","NCRR NIH HHS","U.S. Department of Agriculture","University of Wisconsin-Madison","National Institutes of Health","USDA","NIGMS NIH HHS","NIH HHS","National Science Foundation"],"pagination":["2772-2776"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8486351"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(18)"],"pubmed_abstract":["Assemblies of racemic β-sheet-forming peptides have attracted attention for biomedical applications because racemic forms of peptides can self-associate more avidly than do single enantiomers. In 1953, Pauling and Corey proposed \"rippled β-sheet\" modes of H-bond-mediated interstrand assembly for alternating L- and D-peptide strands; this structural hypothesis was complementary to their proposal of \"pleated β-sheet\" assembly for L-peptides. Although no high-resolution structure has been reported for a rippled β-sheet, there is strong evidence for the occurrence of rippled β-sheets in some racemic peptide assemblies. Here we compare propensities of peptide diastereomers in aqueous solution to form a minimum increment of β-sheet in which two antiparallel strands associate. β-Hairpin folding i"],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Comparisons of β-Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands."],"pmcid":["PMC8486351"],"funding_grant_id":["S10RR025062","S10 RR023438","P41GM136463","S10RR029220","S10 OD012245","OIA-9977486","P41 RR002301","R01GM061238","R01 GM061238","P41RR002301","S10 RR029220","S10RR023438","S10RR08438","DMB-8415048","S10 RR025062","S10RR02781","S10 RR008438","BIR-9214394","P41 GM103399","S10 RR002781","P41 GM136463","P41GM103399"],"pubmed_authors":["Liu X","Gellman SH"],"additional_accession":[]},"is_claimable":false,"name":"Comparisons of β-Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands.","description":"Assemblies of racemic β-sheet-forming peptides have attracted attention for biomedical applications because racemic forms of peptides can self-associate more avidly than do single enantiomers. In 1953, Pauling and Corey proposed \"rippled β-sheet\" modes of H-bond-mediated interstrand assembly for alternating L- and D-peptide strands; this structural hypothesis was complementary to their proposal of \"pleated β-sheet\" assembly for L-peptides. Although no high-resolution structure has been reported for a rippled β-sheet, there is strong evidence for the occurrence of rippled β-sheets in some racemic peptide assemblies. Here we compare propensities of peptide diastereomers in aqueous solution to form a minimum increment of β-sheet in which two antiparallel strands associate. β-Hairpin folding i","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2025-04-04T09:37:18.046Z","creation":"2025-04-04T09:37:18.046Z"},"accession":"S-EPMC8486351","cross_references":{"pubmed":["34288305"],"doi":["10.1002/cbic.202100324"]}}