Please use this identifier to cite or link to this item: http://192.168.98.239:8080/jspui/handle/1994/1327
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dc.date.accessioned2019-02-22T08:18:56Z-
dc.date.available2019-02-22T08:18:56Z-
dc.date.issued2017-11-
dc.identifier.urihttp://192.168.98.239:8080/jspui/handle/1994/1327-
dc.description.abstractAvailableen_US
dc.format.extentxxviii, 191p.en_US
dc.language.isoenen_US
dc.publisherTezpur Universityen_US
dc.relation.ispartofseriesT602;-
dc.subjectMolecular Biology & Biotechnologyen_US
dc.subjectGeriatricsen_US
dc.subjectAlzheimer's diseaseen_US
dc.subjectAmyloid beta-proteinen_US
dc.titleIn silico study on the stuctural dynamics of amyloid-β peptide (Aβ1-42), its aggregation pathway and inhibition : to control the geriatric epidemic, Alzheimer's diseaseen_US
dc.typeThesisen_US
dc.contributor.guideMattaparthi, Venkata Satish Kumar-
dc.creator.researcherDutta, Mary-
dc.departmentDepartment of Molecular Biology & Biotechnologyen_US
Appears in Collections:Theses

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01_title.pdfTitle page1.18 MBAdobe PDFThumbnail
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02_dedication.pdfDedication1.18 MBAdobe PDFThumbnail
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03_abstract.pdfAbstract1.18 MBAdobe PDFThumbnail
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04_declaration.pdfDeclaration by the researcher1.18 MBAdobe PDFThumbnail
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05_certificate.pdfCertificate of the research supervisor1.18 MBAdobe PDFThumbnail
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06_acknowledgement.pdfAcknowledgements1.18 MBAdobe PDFThumbnail
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07_content.pdfTable of contents1.18 MBAdobe PDFThumbnail
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08_chapter1.pdfChapter 1: Motivation & outline of the thesis625.44 kBAdobe PDFThumbnail
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09_chapter2.pdfChapter 2: Introduction & review of literature1.23 MBAdobe PDFThumbnail
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10_chapter3.pdfChapter 3: Methods1.22 MBAdobe PDFThumbnail
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11_chapter4.pdfChapter 4: Investigations on the structural characteristics that seed the aggregation of Aβ1-42 peptide: insights from molecular dynamics simulations1.25 MBAdobe PDFThumbnail
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12_chapter5.pdfChapter 5: Structural characterization of Aβ17-42 peptide dimer by potential of mean force analysis: insights from molecular dynamics simulations1.92 MBAdobe PDFThumbnail
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13_chapter6.pdfChapter 6: Cross-seeding interactions between Amyloid β and Tau protein can enhance aggregation?1.09 MBAdobe PDFThumbnail
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14_chapter7.pdfChapter 7: Examination of the intrinsic disordered regions present in the Aβ1-42 peptide1.23 MBAdobe PDFThumbnail
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15_chap[ter8.pdfChapter 8: Investigation on the interactions stabilizing the Aβ1-42 peptide oligomers and Aβ1-42 fibril polymorphs2.58 MBAdobe PDFThumbnail
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16_chapter9.pdfChapter 9: Inhibition of Aβ1-42 peptide aggregation using short ss-oligonucleotide as polyions: an in silico approach1.47 MBAdobe PDFThumbnail
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17_chapter10.pdfChapter 10: In silico investigation on the inhibition of Aβ1-42 peptide aggregation by Aβ1-40 peptide using potential of mean force study2.04 MBAdobe PDFThumbnail
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18_chapter11.pdfChapter 11: A comparative study to elucidate the inhibitory mechanism of a 6-mer peptide fragment of Aβ1-42 peptide as a potential therapeutic in Alzheimer’s disease1.58 MBAdobe PDFThumbnail
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19_chapter12.pdfChapter 12: Summary and future prospects624.51 kBAdobe PDFThumbnail
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20_bibliography.pdfBibliography750.1 kBAdobe PDFThumbnail
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21_publications.pdfPublications681.48 kBAdobe PDFThumbnail
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