Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/19787
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dc.contributor.authorSrivastava, Shinoo-
dc.contributor.authorSrivastava, Seema-
dc.contributor.authorMelkani, Girish Chandra-
dc.contributor.authorSingh, Shyam-
dc.contributor.authorGupta, Vishwambhar Dayal-
dc.contributor.authorGupta, Vijai Prakash-
dc.date.accessioned2013-07-15T09:47:55Z-
dc.date.available2013-07-15T09:47:55Z-
dc.date.issued2002-12-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/19787-
dc.description410-418en_US
dc.description.abstractThe collective normal modes of the hexapeptide -Ser-Cys-Lys-Leu-Asp-Phe-, a fragment of apolipoprotein B (apo B), have been obtained. They reflect the dynamic nature and are atleast partly responsible for energy input in autolytic activity. Further, on energetic considerations based on the measurements reported by Sim & Sim, it has been shown that of the two such fragments only one induces autolysis, while the other remains anchored to the coated pit.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rightsCC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.39(6) [December 2002]en_US
dc.titleSynthesis, conformation and vibrational dynamics of the peptide -Ser-Cys-Lys-Leu- Asp- Phe-, a fragment of apolipoprotein Ben_US
dc.typeArticleen_US
Appears in Collections: IJBB Vol.39(6) [December 2002]

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