Effects of macromolecular crowding on an intrinsically disordered protein

Hadfield, Andrew (2022) Effects of macromolecular crowding on an intrinsically disordered protein. Memorial University of Newfoundland. (Unpublished)

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Proteins are composed of amino acids, and usually have one native structure. Intrinsically disordered proteins lack a native structure and can populate many different forms, making them ideal for binding. My project is to develop a coarse-grained computational model of an IDP known as ⍺-synuclein, which is found in the brains of Parkinson's disease patients. ⍺-synuclein is an 140 amino acid length protein, and will be modeled using Langevin Dynamics. The free parameters of the model are determined by matching the size of the protein chain, as quantified by the radius of gyration

Item Type: Other
URI: http://research.library.mun.ca/id/eprint/15474
Item ID: 15474
Additional Information: Includes bibliographical references (pages 21-22).
Department(s): Science, Faculty of > Physics and Physical Oceanography
Date: April 2022
Date Type: Submission
Library of Congress Subject Heading: Langevin equations; Macromolecules; Proteins--Analysis.

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