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dc.contributor.authorLeapard, James Brian
dc.date.accessioned2014-03-03T20:20:52Z
dc.date.available2014-03-03T20:20:52Z
dc.date.issued2002-12
dc.identifier.otherleapard_james_b_200212_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/leapard_james_b_200212_ms
dc.identifier.urihttp://hdl.handle.net/10724/20609
dc.description.abstractSurfactant Protein C (SP-C) is one of the two biophysically active proteins in pulmonary surfactant. Bovine SP-C (used in experiments in this thesis) consists of 34 amino acids and is an extremely hydrophobic, predominately á -helical protein of approximately 4.0 kD. Cysteines C4 and C5 are acylated with C-16 (palmitoyl) chains via a thioester linkage. The NMR structure in apolar solvent describes the valine-, leucine- and isoleucine-rich region of this small protein as a rigid rod in which only a few residues near the N terminus (L1 - P7) and the C terminus itself are not helical. It has been recently shown that deacylation causes changes in the structure of the protein and accelerates the formation of amyloid fibrils. Experiments detailed in this thesis show that the deacylated protein is progressively excluded from the monolayer and that the secondary structure changes via a pH dependent mechanism.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectFluorescence microscopy
dc.subjectPulmonary surfactant
dc.subjectSP-C
dc.subjectAmyloid fibrils
dc.subjectAttenuated total reflectance (ATR) Fourier transform infrared spectroscopy
dc.subjectOrientation calculations
dc.titleA custom fluorescence microscope for the observation of surface morphology at the air-water interface and an investigation of surface association and structure of deacylated surfactant protein C
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorRichard A. Dluhy
dc.description.committeeRichard A. Dluhy
dc.description.committeeThomas E. Johnson
dc.description.committeeI. Jon Amster


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