Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1491
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dc.contributor.authorSonar, Mahesh V.en_US
dc.contributor.authorGANESH, KRISHNA N.en_US
dc.date.accessioned2019-01-21T10:29:25Z
dc.date.available2019-01-21T10:29:25Z
dc.date.issued2010-11en_US
dc.identifier.citationOrganic Letters, 12(23).en_US
dc.identifier.issn1523-7060en_US
dc.identifier.issn1523-7052en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/1491-
dc.identifier.urihttps://doi.org/10.1021/ol1021993en_US
dc.description.abstract4S-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.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectUnfolded proteinsen_US
dc.subjectElectron transporten_US
dc.subjectPolyproline peptidesen_US
dc.subjectStereospecific intramolecularen_US
dc.subject2010en_US
dc.titleWater-Induced Switching of β-Structure to Polyproline II Conformation in the 4S-Aminoproline Polypeptide via H-Bond Rearrangementen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleOrganic Lettersen_US
dc.publication.originofpublisherForeignen_US
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