Please use this identifier to cite or link to this item: https://libjncir.jncasr.ac.in/xmlui/handle/10572/2641
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dc.contributor.advisorGovindaraju, T.-
dc.contributor.authorRajasekhar, K.-
dc.date.accessioned2019-07-18T11:08:05Z-
dc.date.available2019-07-18T11:08:05Z-
dc.date.issued2013-
dc.identifier.citationRajasekhar, K. 2013, Synthesis of cyclic hybrid peptoid and peptide based inhibitors for beta-amyloid fibrillar aggregation, MS thesis, Jawaharlal Nehru Centre for Advanced Scientific Research, Bengaluruen_US
dc.identifier.urihttps://libjncir.jncasr.ac.in/xmlui/handle/10572/2641-
dc.description.abstractProteins form the very basis of life, the term protein is derived from the Greek word proteios, which means standing in front. Proteins regulate a variety of activities in all living organisms, from replication of DNA to transport of oxygen across the body. Proteins are responsible for regulating cellular machinery and consequently the phenotype of an organism. Proteins accomplish their task by three-dimensional tertiary and quaternary interactions with various substrates such as DNA, RNA and other proteins. By understanding the structure of the protein, we can probe for its function and potentially apply the new knowledge to various genome and proteome projects, such as mapping the functions of proteins in metabolic pathways and deducing evolutionary relationships and proteome network which is useful in system biology. Peptides1 are short fragments of proteins consists of amino acids linked by amide bonds.2 Peptides can be normally differentiated from proteins by the number of amino acids present in a given chain. Generally a peptide constitutes a minimum of two amino acid residues or a maximum of 50 amino acid residues per chain. Smallest known peptide is a dipeptide followed by tripeptide, tetrapeptide etc.en_US
dc.language.isoEnglishen_US
dc.publisherJawaharlal Nehru Centre for Advanced Scientific Researchen_US
dc.rights© 2013 JNCASR-
dc.subjectPeptide synthesisen_US
dc.titleSynthesis of cyclic hybrid peptoid and peptide based inhibitors for beta-amyloid fibrillar aggregationen_US
dc.typeThesisen_US
dc.type.qualificationlevelMasteren_US
dc.type.qualificationnameMSen_US
dc.publisher.departmentNew Chemistry Unit (NCU)en_US
Appears in Collections:Student Theses (NCU)

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