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DC Field | Value | Language |
---|---|---|
dc.date.accessioned | 2019-02-22T08:18:56Z | - |
dc.date.available | 2019-02-22T08:18:56Z | - |
dc.date.issued | 2017-11 | - |
dc.identifier.uri | http://192.168.98.239:8080/jspui/handle/1994/1327 | - |
dc.description.abstract | Available | en_US |
dc.format.extent | xxviii, 191p. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Tezpur University | en_US |
dc.relation.ispartofseries | T602; | - |
dc.subject | Molecular Biology & Biotechnology | en_US |
dc.subject | Geriatrics | en_US |
dc.subject | Alzheimer's disease | en_US |
dc.subject | Amyloid beta-protein | en_US |
dc.title | In silico study on the stuctural dynamics of amyloid-β peptide (Aβ1-42), its aggregation pathway and inhibition : to control the geriatric epidemic, Alzheimer's disease | en_US |
dc.type | Thesis | en_US |
dc.contributor.guide | Mattaparthi, Venkata Satish Kumar | - |
dc.creator.researcher | Dutta, Mary | - |
dc.department | Department of Molecular Biology & Biotechnology | en_US |
Appears in Collections: | Theses |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
01_title.pdf | Title page | 1.18 MB | Adobe PDF | View/Open |
02_dedication.pdf | Dedication | 1.18 MB | Adobe PDF | View/Open |
03_abstract.pdf | Abstract | 1.18 MB | Adobe PDF | View/Open |
04_declaration.pdf | Declaration by the researcher | 1.18 MB | Adobe PDF | View/Open |
05_certificate.pdf | Certificate of the research supervisor | 1.18 MB | Adobe PDF | View/Open |
06_acknowledgement.pdf | Acknowledgements | 1.18 MB | Adobe PDF | View/Open |
07_content.pdf | Table of contents | 1.18 MB | Adobe PDF | View/Open |
08_chapter1.pdf | Chapter 1: Motivation & outline of the thesis | 625.44 kB | Adobe PDF | View/Open |
09_chapter2.pdf | Chapter 2: Introduction & review of literature | 1.23 MB | Adobe PDF | View/Open |
10_chapter3.pdf | Chapter 3: Methods | 1.22 MB | Adobe PDF | View/Open |
11_chapter4.pdf | Chapter 4: Investigations on the structural characteristics that seed the aggregation of Aβ1-42 peptide: insights from molecular dynamics simulations | 1.25 MB | Adobe PDF | View/Open |
12_chapter5.pdf | Chapter 5: Structural characterization of Aβ17-42 peptide dimer by potential of mean force analysis: insights from molecular dynamics simulations | 1.92 MB | Adobe PDF | View/Open |
13_chapter6.pdf | Chapter 6: Cross-seeding interactions between Amyloid β and Tau protein can enhance aggregation? | 1.09 MB | Adobe PDF | View/Open |
14_chapter7.pdf | Chapter 7: Examination of the intrinsic disordered regions present in the Aβ1-42 peptide | 1.23 MB | Adobe PDF | View/Open |
15_chap[ter8.pdf | Chapter 8: Investigation on the interactions stabilizing the Aβ1-42 peptide oligomers and Aβ1-42 fibril polymorphs | 2.58 MB | Adobe PDF | View/Open |
16_chapter9.pdf | Chapter 9: Inhibition of Aβ1-42 peptide aggregation using short ss-oligonucleotide as polyions: an in silico approach | 1.47 MB | Adobe PDF | View/Open |
17_chapter10.pdf | Chapter 10: In silico investigation on the inhibition of Aβ1-42 peptide aggregation by Aβ1-40 peptide using potential of mean force study | 2.04 MB | Adobe PDF | View/Open |
18_chapter11.pdf | Chapter 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 disease | 1.58 MB | Adobe PDF | View/Open |
19_chapter12.pdf | Chapter 12: Summary and future prospects | 624.51 kB | Adobe PDF | View/Open |
20_bibliography.pdf | Bibliography | 750.1 kB | Adobe PDF | View/Open |
21_publications.pdf | Publications | 681.48 kB | Adobe PDF | View/Open |
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