UMD Theses and Dissertations

Permanent URI for this collectionhttp://hdl.handle.net/1903/3

New submissions to the thesis/dissertation collections are added automatically as they are received from the Graduate School. Currently, the Graduate School deposits all theses and dissertations from a given semester after the official graduation date. This means that there may be up to a 4 month delay in the appearance of a given thesis/dissertation in DRUM.

More information is available at Theses and Dissertations at University of Maryland Libraries.

Browse

Filters

20191

Settings

Author: search.filters.author.Tammareddy, TejaswiSubject: search.filters.subject.lipid bilayer

Search Results

Now showing 1 - 1 of 1
  • Thumbnail Image
    Item
    EFFECT OF LIPID-PROTEIN INTERACTIONS ON THE CONDUCTANCE OF THE TRANSMEMBRANE PROTEIN ALPHA HEMOLYSIN USING MOLECULAR DYNAMICS SIMULATIONS
    (2019) Tammareddy, Tejaswi; Klauda, Jeffery; Chemical Engineering; Digital Repository at the University of Maryland; University of Maryland (College Park, Md.)
    Alpha-hemolysin (aHL) is a transmembrane ion-conducting channel which finds application in single molecule sensing using nanopore technology. Biomolecules are allowed to pass through the pore of the protein and, as a result, there is a change in the ion current, which is monitored to quantify single-molecule sensing. However, it has been established that the change in current is also affected by the lipid membrane in which the protein is present. It is also known that cholesterol has a concentration-dependent reduction in the current through the pore, experimentally. The understanding of current reduction at a single-molecule level and theoretical models replicating these conditions are lacking. In the current thesis, molecular dynamics simulations are performed on aHL inserted into a 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-choline (POPC) lipid bilayer with varying concentrations of cholesterol to investigate the effect on ionic current. Effect of lipid interactions, especially of cholesterol, on the protein structure and hence functioning of the ion channel is investigated