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Conformational study of small peptides using spectroscopy and quantum chemistry calculations

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dc.contributor.advisor DAS, ALOKE en_US
dc.contributor.author R.S., KAARTHIK en_US
dc.date.accessioned 2020-06-11T10:02:27Z
dc.date.available 2020-06-11T10:02:27Z
dc.date.issued 2020-05 en_US
dc.identifier.uri http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4675
dc.description.abstract Structure-function relationship found in protein helps us to understand the function that a protein is capable of by knowing its structure. Following the secondary structure of a small peptide will give more information on the structure of the protein, which can be used to understand the functions of the protein in detail. Apart from covalent bonds, these secondary structures are shaped by non-covalent interactions like hydrogen bonds, hydrophobic interactions, and n→π* interactions. Though these non-covalent interactions are individually weak, many such interactions cumulatively contribute to stabilising the conformation of a peptide. Gas-phase studies on small peptides are carried out to study such non-covalent interactions that are supporting the peptides when there is no effect from the solvent medium or any other nearby molecules. en_US
dc.language.iso en en_US
dc.subject Peptides en_US
dc.subject Double resonance spectroscopy en_US
dc.subject Amino acids en_US
dc.subject Quantum chemistry en_US
dc.subject Ultraviolet lasers en_US
dc.subject 2020 en_US
dc.title Conformational study of small peptides using spectroscopy and quantum chemistry calculations en_US
dc.type Thesis en_US
dc.type.degree BS-MS en_US
dc.contributor.department Dept. of Chemistry en_US
dc.contributor.registration 20151014 en_US


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  • MS THESES [1705]
    Thesis submitted to IISER Pune in partial fulfilment of the requirements for the BS-MS Dual Degree Programme/MSc. Programme/MS-Exit Programme

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