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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sonar, Mahesh V. | en_US |
dc.contributor.author | GANESH, KRISHNA N. | en_US |
dc.date.accessioned | 2019-01-21T10:29:25Z | |
dc.date.available | 2019-01-21T10:29:25Z | |
dc.date.issued | 2010-11 | en_US |
dc.identifier.citation | Organic Letters, 12(23). | 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/123456789/1491 | - |
dc.identifier.uri | https://doi.org/10.1021/ol1021993 | en_US |
dc.description.abstract | 4S-Aminoproline polypeptide 2 forms unusual β-structure in trifluoroethanol that switches to the polyproline II (PPII) form in aqueous medium, while 4R-aminoproline peptide 1 retains PPII form in both solvents. This first instance of a polyproline derivative showing a β-structure is attributed to competitive pH-dependent (4-NH3+/NH2) stereoelectronic effect (4R vs 4S) and the overriding importance of stereospecific intra/intermolecular H-bonding in (2,4)-cis-4S-aminoproline in contrast to (2,4)-trans-4R-aminoproline oligomers. | en_US |
dc.language.iso | en | en_US |
dc.publisher | American Chemical Society | en_US |
dc.subject | Unfolded proteins | en_US |
dc.subject | Electron transport | en_US |
dc.subject | Polyproline peptides | en_US |
dc.subject | Stereospecific intramolecular | en_US |
dc.subject | 2010 | en_US |
dc.title | Water-Induced Switching of β-Structure to Polyproline II Conformation in the 4S-Aminoproline Polypeptide via H-Bond Rearrangement | 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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