• Find People
  • Campus Map
  • PiratePort
  • A-Z
    • About
    • Submit
    • Browse
    • Login
    View Item 
    •   ScholarShip Home
    • Academic Affairs
    • Thomas Harriot College of Arts and Sciences
    • Chemistry
    • View Item
    •   ScholarShip Home
    • Academic Affairs
    • Thomas Harriot College of Arts and Sciences
    • Chemistry
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of The ScholarShipCommunities & CollectionsDateAuthorsTitlesSubjectsTypeDate SubmittedThis CollectionDateAuthorsTitlesSubjectsTypeDate Submitted

    My Account

    Login

    Statistics

    View Google Analytics Statistics

    A Molecular Dynamics Study into Annexin A1 Induced Membrane Binding and Aggregation

    Thumbnail
    View/ Open
    Donohue_ecu_0600M_10244.pdf (11.15Mb)

    Show full item record
    Author
    Donohue, Matthew P.
    Abstract
    Annexins constitute a family of proteins that bind to anionic membranes in a reversible and calcium dependent manner through the unique architecture of their calcium binding sites. In addition, annexins with relatively large N-terminal domains have been identified to cause membrane aggregation and fusion. There is a contradiction between x-ray crystallography and cryo-EM studies as to the proposed mechanism of annexin-induced membrane aggregation.  Molecular dynamics simulations were performed in an effort to study the calcium dependent binding of annexin I to a phospholipid bilayer and to investigate the N-terminus as a possible second membrane binding site. Site specific mutations were created on the N-terminus to study the effects phosphorylation has on the tertiary structure of the protein. Simulation trajectories were analyzed in terms of non-bonded interaction energies of protein residues, root mean square deviations of the protein backbone, root mean square fluctuations of residues and nuclear distances between calcium ions and their oxygen ligands. Calcium coordination with lipid headgroups was observed in repeat IV of the core domain. Two lysine residues located in the N-terminus and speculated to be crucial to membrane aggregation displayed significant electrostatic   attractions to the phospholipid layer based on MM-PBSA calculations. This thesis will present a model for the mechanism of interaction between annexin A1 and membranes.  
    URI
    http://hdl.handle.net/10342/2915
    Subject
     Chemistry, Physical; Physical chemistry 
    Date
    2010
    Citation:
    APA:
    Donohue, Matthew P.. (January 2010). A Molecular Dynamics Study into Annexin A1 Induced Membrane Binding and Aggregation (Master's Thesis, East Carolina University). Retrieved from the Scholarship. (http://hdl.handle.net/10342/2915.)

    Display/Hide MLA, Chicago and APA citation formats.

    MLA:
    Donohue, Matthew P.. A Molecular Dynamics Study into Annexin A1 Induced Membrane Binding and Aggregation. Master's Thesis. East Carolina University, January 2010. The Scholarship. http://hdl.handle.net/10342/2915. March 02, 2021.
    Chicago:
    Donohue, Matthew P., “A Molecular Dynamics Study into Annexin A1 Induced Membrane Binding and Aggregation” (Master's Thesis., East Carolina University, January 2010).
    AMA:
    Donohue, Matthew P.. A Molecular Dynamics Study into Annexin A1 Induced Membrane Binding and Aggregation [Master's Thesis]. Greenville, NC: East Carolina University; January 2010.
    Collections
    • Chemistry
    • Master's Theses
    Publisher
    East Carolina University

    xmlui.ArtifactBrowser.ItemViewer.elsevier_entitlement

    East Carolina University has created ScholarShip, a digital archive for the scholarly output of the ECU community.

    • About
    • Contact Us
    • Send Feedback