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Length-dependent stability and strand length limits in antiparallel -sheet secondary structure
2001
Proceedings of the National Academy of Sciences of the United States of America
Designed peptides that fold autonomously to specific conformations in aqueous solution are useful for elucidating protein secondary structural preferences. For example, autonomously folding model systems have been essential for establishing the relationship between ␣-helix length and ␣-helix stability, which would be impossible to probe with ␣-helices embedded in folded proteins. Here, we use designed peptides to examine the effect of strand length on antiparallel -sheet stability. ␣-Helices
doi:10.1073/pnas.211536998
pmid:11593011
pmcid:PMC59824
fatcat:7d5h57k7erhq5mpy4wzu7eruwq