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dc.contributor.advisorMubassir, M H M
dc.contributor.authorAlvy, Raghib Ishraq
dc.date.accessioned2021-10-03T05:12:37Z
dc.date.available2021-10-03T05:12:37Z
dc.date.copyright2021
dc.date.issued2021-01
dc.identifier.otherID: 20376005
dc.identifier.urihttp://hdl.handle.net/10361/15091
dc.descriptionThis thesis report is submitted in partial fulfillment of the requirement for the degree of Master of Science in Biotechnology, 2021.en_US
dc.descriptionCatalogued from PDF version of thesis.
dc.descriptionIncludes bibliographical references (pages 95-103).
dc.description.abstractPattern Triggered Immunity (PTI) is distinguished with the activities of pattern recognition receptors (PRRs), which play an essential role in plant defense mechanism. During aggression of microbes, PRRs immediately bind with the PAMPs and recruit co-receptors to initiate the defense signal. Several plant PRRs have been discovered, very few of their functional parameters have been studied. In this study, the crystallographic structures of FLS2-flg22-BAK1 (PDB ID: 4MN8), HAESA-IDA-SERK1 (PDB ID: 5IYX) and PSKR-Phytosulphokine-SERK1 (PDB ID: 4Z64) complexes were simulated for 30ns. Simulated trajectories were analyzed for getting an overview of the immune response of PRRs towards PAMPs with the help of co-receptors. Moreover, MM/PBSA calculation revealed that interaction between FLS2-BAK1 and HAESA-SERK1 show similarity whereas PSKR interacts differently with SERK1. As PRRs play a major role in plant defense mechanism, it can be hypothesized that binding mechanism with PAMPs and co-receptors will help to understand the interaction pattern of PTI.en_US
dc.description.statementofresponsibilityRaghib Ishraq Alvy
dc.format.extent104 Pages
dc.language.isoen_USen_US
dc.publisherBrac Universityen_US
dc.rightsBrac University theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission.
dc.subjectPattern Triggered Immunityen_US
dc.subjectPattern Recognition Receptorsen_US
dc.subjectMM/PBSAen_US
dc.subjectPAMPen_US
dc.subjectMolecular Dynamicsen_US
dc.subjectBioinformaticsen_US
dc.titleStructural analysis of three pivotal SERK dependent PRR complexes of Arabidopsis thalianaen_US
dc.typeThesisen_US
dc.contributor.departmentDepartment of Mathematics and Natural Sciences, Brac University
dc.description.degreeM. Biotechnology


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