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Molecular Mechanic Studies on the Zwitterionic and Neutral Conformation Stability of Biological Active Peptide

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dc.creator KECEL GUNDUZ, Serda
dc.creator CELIK, Sefa
dc.date 2017-10-24T00:00:00Z
dc.date.accessioned 2019-07-09T11:59:33Z
dc.date.available 2019-07-09T11:59:33Z
dc.identifier http://dergipark.org.tr/sdufenbed/issue/34610/382233
dc.identifier 10.19113/sdufbed.02983
dc.identifier.uri http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/46339
dc.description In this current work the conformational properties of the L-Alanyl-L-Glutamine dipeptide which was biological active dipeptide has been investigated by theoretical conformational analysis method using program which is based on Molecular Mechanic calculations in order to determine the structure function relation. The calculations on zwitterionic and neutral form of Ala-Gln which is formed side and main chain torsion angles let us to define their preferable energetically conformers. The side and main chain status of the stable conformations of Ala-Gln were acquired based on the results of the conformational analysis. By using Ramachandran maps, the global conformation, which has the lowest energy of the dipeptide, has been determined. The goal of this work was to explain structure-activity relationship by investigating the bioactive conformation of biological active peptide.
dc.format application/pdf
dc.publisher Süleyman Demirel University
dc.publisher Süleyman Demirel Üniversitesi
dc.relation http://dergipark.org.tr/download/article-file/408873
dc.source Volume: 21, Issue: 3 836-842 en-US
dc.source 1308-6529
dc.subject Zwitterionic,Neutral; Ala-Gln; Conformational analysis; DFT
dc.title Molecular Mechanic Studies on the Zwitterionic and Neutral Conformation Stability of Biological Active Peptide en-US
dc.type info:eu-repo/semantics/article


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