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dc.contributor.advisorViswamitra, M A
dc.contributor.authorNeela, H Y
dc.date.accessioned2026-02-12T05:13:21Z
dc.date.available2026-02-12T05:13:21Z
dc.date.submitted1992
dc.identifier.urihttps://etd.iisc.ac.in/handle/2005/8626
dc.description.abstractThe database analysis thus interestingly shows that the conformation observed at the active site in CLPA and antamanide is a preferred conformation observed in other oligopeptides and proteins as well. From the Leu–Leu analyses we can conclude that although the conformation of oligopeptides in crystals is severely constrained by strong packing forces, specific geometries of weak interactions still exist.
dc.language.isoen_US
dc.relation.ispartofseriesT03192
dc.rightsI grant Indian Institute of Science the right to archive and to make available my thesis or dissertation in whole or in part in all forms of media, now hereafter known. I retain all proprietary rights, such as patent rights. I also retain the right to use in future works (such as articles or books) all or part of this thesis or dissertation
dc.subjectOligopeptide Conformation
dc.subjectWeak Interactions
dc.subjectProtein Structural Analysis
dc.titleX-ray crystallographic studies of a cytoprotective agent cyclolinopeptide: a cyclic nanopeptide
dc.typeThesis
dc.degree.levelDoctoral
dc.degree.grantorIndian Institute of Science
dc.degree.disciplineScience


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