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dc.contributor.advisorSpreter, Thomas
dc.contributor.authorBerryman, Meghan A.
dc.date.accessioned2018-04-07T16:58:49Z
dc.date.available2018-04-07T16:58:49Z
dc.date.issued2009
dc.identifier.urihttp://hdl.handle.net/10920/34745
dc.description30 p.en_US
dc.description.abstractSalmonella is a bacterial pathogen responsible for food-born gastroenteritis and typhoid fever in humans. The pathogen modulates pre-established signaling cascades within the host cell using its own macromolecular protein structure, Type III Secretion System (T3SS), that sits within the layers of the bacterial cell membrane and penetrates the host cell by creating a pore in its surface. This allows Salmonella to inject virulence proteins, called effector proteins, directly into the host cell. Inositol phosphate phosphatase SopB is one of the key effector proteins. Through indirect stimulus of guanosine triphosphatases (GTPases) Cdc42 and Rac, SopB triggers actin cytoskeleton rearrangements and membrane ruffling, cellular effects characteristic of Salmonella infection. Previous scientists have been unsuccessful in attempts to purify and stabilize protein SopB for crystallographic analysis. This study modified the protocol for purification. These modifications allowed for the protein to spend as little time as possible in unstable environments, such as extreme temperature change, while the process of purification was underway. This approach was successful in purifying and concentrating SopB and Cdc42 protein complex for use in recrystal study.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Chemistry Senior Individualized Projects Collection
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved.
dc.titleBiochemical Analysis of Salmonella Type III Secretion System Effector Protein SopBen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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  • Chemistry Senior Individualized Projects [860]
    This collection includes Senior Individualized Projects (SIP's) completed in the Chemistry Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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