Vibrational circular dichroism and its applications to structural studies in peptides.
Item
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Title
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Vibrational circular dichroism and its applications to structural studies in peptides.
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Identifier
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AAI9530930
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identifier
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9530930
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Creator
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Xie, Ping.
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Contributor
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Adviser: Max Diem
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Date
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1995
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Language
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English
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Publisher
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City University of New York.
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Subject
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Chemistry, Physical | Biophysics, General | Chemistry, Biochemistry
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Abstract
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This dissertation reportes recent progress in vibrational circular dichroism (CD) and its application to the measurement of secondary structure of peptide. It is focused on two aspects: elimination of artifact in VCD measurement and structural studies of small peptides.;System artifact has limited application of biomolecule structural studies, because its small amplitude of {dollar}\Delta{dollar}A in vibrational CD. Such an artifact can arise from both hardware and software. The new method of data acquisition and processing proposed can largely reduce such an artifact. Results from new method shows a same pattern of poly-L-lysine in DMSO at low concentration (0.05 absorbance unit) as it in high concentration.;Conformational changes of several small peptides with various chemical environment are monitored by VCD. Such environment variations can be polarity and hydrogen-bond ability of solvent as well as size and charge of cation. The variety of solvent properties can be as a probe, which can help us to understand the driving force in peptide folding. The frequency strategy of VCD is employed in interpreting such structural changes. Structures from such an analysis consist with that from other techniques. The computed spectra based on COM model further confirmed structures from observed VCD.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
