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dc.contributor.authorHuy X. Luong-
dc.contributor.authorYoung-Woo Kim-
dc.date.accessioned2020-10-13T04:18:12Z-
dc.date.available2020-10-13T04:18:12Z-
dc.date.issued2020-
dc.identifier.urihttps://pubs.acs.org/doi/10.1021/acs.orglett.0c02914-
dc.identifier.urihttps://dlib.phenikaa-uni.edu.vn/handle/PNK/586-
dc.description.abstractPolyproline II helix (PPII) is one of the secondary structures in proteins that play an important role in various biological processes. In this study, we have developed a new macrocyclization strategy that efficiently reinforces a model tetrapeptide into a PPII structure. We also elucidated some relationships between structural features and PPII stability in this model. This new macrocyclic stapling strategy can serve as a useful chemical tool to manipulate the PPII structure for various applications.vi
dc.language.isoenvi
dc.publisherACS Publicationsvi
dc.subjectPeptides and proteinsvi
dc.subjectCircular dichroism spectroscopy,vi
dc.subjectChemical structurevi
dc.subjectMetathesisvi
dc.subjectNucleic acid structurevi
dc.titleStabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staplesvi
dc.typeArticlevi
dc.typeWorking Papervi
eperson.identifier.doihttps://doi.org/10.1021/acs.orglett.0c02914-
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