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http://hdl.handle.net/10603/428841
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DC Field | Value | Language |
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dc.date.accessioned | 2022-12-20T10:21:03Z | - |
dc.date.available | 2022-12-20T10:21:03Z | - |
dc.identifier.uri | http://hdl.handle.net/10603/428841 | - |
dc.description.abstract | The work reported in this thesis is focused on understanding the conformational properties of peptide foldamers containing and#946; or and#947; amino acid residues. Chapter 1 includes a brief state-of-the-art literature review on peptide foldamers containing and#946; and/or and#947; amino acids. Chapter 2 describes the effect of insertion of an Aib residue in a and#946;3(R) peptide sequence with the help of two model peptides of comparable length- Boc-[and#946;3(R)Val]9-OMe and Boc-[(and#946;3(R)Val)3-Aib-(and#946;3(R)Val)4]-OMe. Results in chapter 2 demonstrate the influence of the gem-dimethyl effect of Aib residues on the conformation of Aib/and#946;3(S) peptides. In principle, the nature and chirality of the component residues also might affect the conformation of the heterogeneous peptides. Chapter 3 attempts to demonstrate a few of such effects with the help of NMR studies on few model peptides- (Boc-(Val)2-Ala-(Leu)2-OMe, Boc-(Val)2-and#946;3(S)Ala-(Leu)2-OMe, Boc-(Val)2-and#947;4(S)Ala-(Leu)2-OMe, Boc-Val-DVal-and#946;3(S)Ala-(Leu)2-OMe and Boc-Val-DVal-and#947;4(S)Ala-(Leu)2-OMe) and with a crystal structure database (CSD) analysis. Chapter 4 reports the first solution state structural characterization of C12/C14/C12 helices in peptides of the type- [and#947;4(R)-Aib-and#947;4(R)]2 and [and#947;4(R)-and#945;(L)-and#947;4(R)]2. and#916;and#948; values of amide NHs (from DMSO-d6 titration in CDCl3) in the hexapeptides used in this study, as well as the hydrogen bond parameters and some other features of the crystal structures, reported in a previous study consistently and conclusively points to the existence of the hydrogen bond heterogeneity in C12/C14/C12 helix. Chapter 5 demonstrates the effect of insertion of a DPro-Gly segment in a and#947;4(R) peptide sequence using three model peptides- Boc-and#947;4(R)Leu-and#947;4(R)Leu-and#947;4(R)Leu-and#947;4(R)Leu-DPro-Gly-and#947;4(R)Leu-and#947;4(R)Leu-and#947;4(R)Leu-and#947;4(R)Leu-OMe, Boc-and#947;4(R)Ile-and#947;4(R)Ile-and#947;4(R)Ile-and#947;4(R)Ile -DPro-Gly-and#947;4(R)Ile-and#947;4(R)Ile-and#947;4(R)Ile-and#947;4(R)Ile-OMe and Boc-and#947;4(R)Val-and#947;4(R)Val-and#947;4(R)Val-and#947;4(R)Val-DPro-Gly-and#947;4(R)Val-and#947;4(R)Val-and#947;4(R)Val-and#947;4(R)Val-OMe. | - |
dc.language | English | - |
dc.rights | university | - |
dc.title | Structural Insights into Peptide Foldamers Containing β or γ Amino Acid Residues Gained Using NMR Spectroscopy | - |
dc.creator.researcher | George, Gijo | - |
dc.subject.keyword | Physical Sciences | - |
dc.subject.keyword | Physics | - |
dc.subject.keyword | Physics Multidisciplinary | - |
dc.contributor.guide | Raghothama, S and Ramesh, K P | - |
dc.publisher.place | Bangalore | - |
dc.publisher.university | Indian Institute of Science Bangalore | - |
dc.publisher.institution | Physics | - |
dc.date.completed | 2021 | - |
dc.date.awarded | 2021 | - |
dc.format.dimensions | 30cm | - |
dc.format.accompanyingmaterial | None | - |
dc.source.university | University | - |
dc.type.degree | Ph.D. | - |
Appears in Departments: | Physics |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
01_title.pdf | Attached File | 143.03 kB | Adobe PDF | View/Open |
02_prelim pages.pdf | 350.81 kB | Adobe PDF | View/Open | |
03_contents.pdf | 85.89 kB | Adobe PDF | View/Open | |
04_abstract.pdf | 341.82 kB | Adobe PDF | View/Open | |
05_chapter 1.pdf | 583.18 kB | Adobe PDF | View/Open | |
06_chapter 2.pdf | 1.85 MB | Adobe PDF | View/Open | |
07_chapter 3.pdf | 2.01 MB | Adobe PDF | View/Open | |
08_chapter 4.pdf | 1.99 MB | Adobe PDF | View/Open | |
09_chapter 5.pdf | 1.56 MB | Adobe PDF | View/Open | |
10_annexure.pdf | 210.32 kB | Adobe PDF | View/Open | |
80_recommendation.pdf | 1.71 MB | Adobe PDF | View/Open |
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