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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Huy X. Luong | - |
| dc.contributor.author | Young-Woo Kim | - |
| dc.date.accessioned | 2020-10-13T04:18:12Z | - |
| dc.date.available | 2020-10-13T04:18:12Z | - |
| dc.date.issued | 2020 | - |
| dc.identifier.uri | https://pubs.acs.org/doi/10.1021/acs.orglett.0c02914 | - |
| dc.identifier.uri | https://dlib.phenikaa-uni.edu.vn/handle/PNK/586 | - |
| dc.description.abstract | Polyproline 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.iso | en | vi |
| dc.publisher | ACS Publications | vi |
| dc.subject | Peptides and proteins | vi |
| dc.subject | Circular dichroism spectroscopy, | vi |
| dc.subject | Chemical structure | vi |
| dc.subject | Metathesis | vi |
| dc.subject | Nucleic acid structure | vi |
| dc.title | Stabilization of Single Turn Polyproline II Helices via Macrocyclic Hydrocarbon Staples | vi |
| dc.type | Article | vi |
| dc.type | Working Paper | vi |
| eperson.identifier.doi | https://doi.org/10.1021/acs.orglett.0c02914 | - |
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