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dc.contributor.advisorBalaram, P
dc.contributor.authorSonti, Rajesh
dc.date.accessioned2018-04-05T03:02:49Z
dc.date.accessioned2018-07-30T14:27:35Z
dc.date.available2018-04-05T03:02:49Z
dc.date.available2018-07-30T14:27:35Z
dc.date.issued2018-04-05
dc.date.submitted2013
dc.identifier.urihttp://etd.iisc.ac.in/handle/2005/3335
dc.identifier.abstracthttp://etd.iisc.ac.in/static/etd/abstracts/4200/G25727-Abs.pdfen_US
dc.description.abstractThis thesis describes NMR studies which probe weak interactions between amino acid side chains in folded peptide structures. Aromatic/aromatic interactions between facing phenylalanine residues have been probed in antiparallel β-sheets, while aromatic/proline interactions have been examined using cyclic peptide disulfides that occur in the venom of marine cone snails. Novel intramolecular hydrogen bonded structures in hybrid peptides containing backbone homologated residues, specifically γ-amino acids, are also described. Chapter 1 provides a brief background to the principles involved in the design of antiparallel β-sheet structures and an introduction to previous studies on aromatic/aromatic and aromatic/proline interactions in influencing peptide conformations. A summary of the NMR methods used is also presented. Chapter 2 discusses the structural characterisation of a designed 14 residue, three stranded β-sheet peptide, Boc-LFVDP-PLFVADP-PLFV-OMe (LFV14). The results described in this Chapter support the presence of multiple conformational states about the χ1 (Cα-Cβ) torsional degree of freedom for the interacting aromatic pairs in solution. Chapter 3 presents the structural characterisation of a designed 19 residue three stranded hybrid β-sheet peptide, Boc-LVβFVDPGLβFVVLDPGLVLβFVV-OMe (BBH19). β-amino acid residues (β-phenylalanine, βPhe) were incorporated at facing positions on antiparallel β-sheets. The BBH19 structure provides an example of interaction between the N and C-terminal strands in a three stranded structure with an α/β hybrid backbone. Chapter 4 focuses on studies of the conformations of the contryphan In936 (GCVDLYPWC*) from Conus inscriptus and the related peptide Lo959 (GCPDWDPWC*) from Conus loroissi. Both peptides possess a macrocyclic 23 membered ring, with multiple accessible conformational states. Chapter 5 describes conformational analysis of a novel 20 membered cyclic peptide disulfide, CIWPWC (Vi804), from Conus virgo. NMR structures were calculated for Vi804 and an analog peptide, CIDWPWC, DW3-Vi804. Chapter 6 explores the solution conformation of hybrid sequences containing α and γ residues. Oligopeptides of the type (αγ)n and (αγγ)n have been studied in solution by NMR methods. Chapter 7 provides a summary of the results described in this thesis and highlights the major conclusions.en_US
dc.language.isoen_USen_US
dc.relation.ispartofseriesG25727en_US
dc.subjectNatural Peptidesen_US
dc.subjectAromatic/Aromatic Interactionsen_US
dc.subjectAromatic/Proline Interactionsen_US
dc.subjectPeptides - Conformational Analysisen_US
dc.subjectNuclear Magnetic Resonanceen_US
dc.subjectCyclic Peptide Disulfidesen_US
dc.subjectCyclic Peptidesen_US
dc.subjectHybrid Peptidesen_US
dc.subjectBeta Hairpinsen_US
dc.subjectBeta Sheetsen_US
dc.subjectCyclic Peptide Disulfidesen_US
dc.subjectDesigned Peptidesen_US
dc.subjectProteins - Analysisen_US
dc.subjectβ-Hairpinen_US
dc.subjectβ-sheet Peptideen_US
dc.subjectα/β Hybrid Peptideen_US
dc.subject.classificationBiochemistryen_US
dc.titleConformational Analysis of Designed and Natural Peptides : Studies of Aromatic/Aromatic and Aromatic/Proline Interactions by NMRen_US
dc.typeThesisen_US
dc.degree.namePhDen_US
dc.degree.levelDoctoralen_US
dc.degree.disciplineFaculty of Scienceen_US


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