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dc.creatorNandkumar, Rohan
dc.date.available2013-08-27T19:54:47Z
dc.date.issued2013-08
dc.identifier.urihttp://hdl.handle.net/2346/50306
dc.description.abstractMuscle cells undergo frequent damage and repair, which is an essential process to maintain cellular homeostasis. These processes involve plasma membrane repair and remodeling following damage. The inability of a cell to repair membrane lesions can lead to pathological conditions such as muscular dystrophy and cardiovascular diseases. Mitsugumin 53 (MG53) is a muscle-specific protein belonging to the tripartite motif (TRIM 72) family of proteins. MG53 primarily interacts with phosphatidylserine, a phospholipid that specific to the inner leaflet of the plasma membrane and cytoplasmic face of intracellular vesicles. Interactions between MG53 and dysferlin are also thought to play a role in membrane repair. This work describes the analysis of MG53 using Isothermal Titration Calorimetry (ITC), Fourier Transform Infrared (FTIR) spectroscopic analysis and Circular Dichroism (CD). These techniques are capable of measuring the thermodynamic properties that describe the interactions between MG53 and potential ligands, such as o-phosphoserine and dysferlin. The ultimate goal is to better understand the role of MG53 and its contribution to membrane repair.
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.subjectMitsugumin 53
dc.subjectMembrane repair
dc.subjectPhosphatidylserine
dc.subjectO-phosphoserine
dc.titleBiophysical characterization of Mitsugumin 53 protein
dc.typeThesis
thesis.degree.nameMaster of Science
thesis.degree.levelMasters
thesis.degree.disciplineBiotechnology
thesis.degree.grantorTexas Tech University
thesis.degree.departmentBiotechnology
dc.contributor.committeeMemberKnaff, David B.
dc.contributor.committeeMemberKottapalli, Kameswara Rao
dc.contributor.committeeChairSutton, Bryan R
dc.rights.availabilityUnrestricted.


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