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Toward determining amyloid fibril structures using experimental constraints from Raman spectroscopy

Harper, Maddie
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Abstract
Amyloid fibrils are β-sheet rich protein aggregates that are implicated in diseases such as Alzheimer’s. Using Raman Spectroscopy, we demonstrated the distributions of peptide backbone amide C=O bond orientation and Ramachandran ψ dihedral angles can effectively guide molecular dynamics (MD) simulations to build structural models of amyloid fibrils. Our model systems, amylin20−29 and amyloid-β (Aβ)25−35, are oriented inextended β-sheet strands that are either parallel (amylin20−29 and Aβ25−35) or antiparallel (amylin20−29) β-sheet structures. Overall, our work lays the foundation for utilizing Raman spectroscopy as structural constraints in MD simulations to determine the three-dimensional molecular structural models of amyloid fibrils.
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Date
2024-01-01
Student Status
Graduate
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Type of presentation
Poster Presentation
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UVM Student Research Conference
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URI
https://hdl.handle.net/20.500.14849/8697
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Advisor(s)
David Punihaole
Department
Program/Major
Chemistry
College/School
College of Arts and Sciences
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Physical Science
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