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dc.contributor.advisorHong, Heedeok
dc.contributor.authorChien, Christine L.
dc.descriptionv, 21 p.en_US
dc.description.abstractMembrane proteins (MPs) carry out crucial molecular processes in living organisms including energy generation, molecular signaling, and catalysis. The folding of MPs is directly connected to human health. Misfolded MPs are known to cause fatal diseases such as cystic fibrosis, Alzheimer’s disease, and cancer. Although protein folding has been studied extensively in hydrophilic proteins, the same cannot be said about MPs. This is due to limitations in current methods used to study reversible folding in hydrophobic environments such as the lipid bilayer. The knowledge gap may be too expansive to narrow, but this important protein class cannot be overlooked and therefore new techniques to study MP folding kinetics are needed. Investigating such techniques will provide important information about structure prediction and the design of innovative MPs for pharmaceutical practices. These methods are based on steric trapping, where unfolding of biotinylated proteins is linked to the competitive binding of monovalent streptavidin (mSA). This method is utilized to investigate the thermodynamic stability of MPs in native conditions without the use of temperature, pulling force, or chemical denaturants. In this study, GlpG was isolated from E. coli and subject to steric trapping. Steric trapping is widely applicable to different types of MP systems, including non-functional and misfolded variants. Thus, the findings in this study will provide insight to the folding energy landscape of MPs.en_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.titleElucidating Protein Folding Mechanics of Membrane-Bound GlpG in E. coli through Steric Trappingen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email 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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