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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Kumar, Mothukuri Ganesh | en_US |
| dc.contributor.author | MALI, SACHITANAND M. | en_US |
| dc.contributor.author | Raja, K. Muruga Poopathi | en_US |
| dc.contributor.author | GOPI, HOSAHUDYA N. | en_US |
| dc.date.accessioned | 2019-03-15T11:22:37Z | |
| dc.date.available | 2019-03-15T11:22:37Z | |
| dc.date.issued | 2015-01 | en_US |
| dc.identifier.citation | Organic Letters, 17 (2), 230-233. | en_US |
| dc.identifier.issn | 1523-7060 | en_US |
| dc.identifier.issn | 1523-7052 | en_US |
| dc.identifier.uri | http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/2145 | - |
| dc.identifier.uri | https://doi.org/10.1021/ol503310r | en_US |
| dc.description.abstract | The synthesis and utilization of novel thiostatines (β-SH-substituted γ-amino acids) in the design of backbone-disulfide-stabilized β-hairpin mimetics, solution conformations of hybrid β-hairpins and Cys-disulfide-stabilized α-peptide analogue, their thiol exchange, and proteolytic stability are investigated. The results suggest that thiostatines can be used to design proteolytically stable water-soluble β-hairpin mimetics without deviating from overall β-hairpin conformation. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | American Chemical Society | en_US |
| dc.subject | Design of Stable β-Hairpin | en_US |
| dc.subject | Disulfide Bonds | en_US |
| dc.subject | Stable protein secondary structure | en_US |
| dc.subject | Antimicrobial peptides | en_US |
| dc.subject | 2015 | en_US |
| dc.title | Design of Stable β-Hairpin Mimetics through Backbone Disulfide Bonds | en_US |
| dc.type | Article | en_US |
| dc.contributor.department | Dept. of Chemistry | en_US |
| dc.identifier.sourcetitle | Organic Letters | en_US |
| dc.publication.originofpublisher | Foreign | en_US |
| Appears in Collections: | JOURNAL ARTICLES | |
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