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Electrophilic and acid catalysis in nucleophilic aromatic substitutions林啓標, Lam, Kai-biu. January 1967 (has links)
published_or_final_version / Chemistry / Master / Master of Science
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THE HYDROBORATION OF 7-AZAINDOLE, 1,8-NAPHTHYRIDINE, AND THEIR N-METHYLATED DERIVATIVES.Piepgrass, Kent Wesley. January 1982 (has links)
No description available.
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Stereochemical and mechanistic studies on 2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolaseLam, Winnie Wai Yin January 1995 (has links)
No description available.
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X-ray diffraction studies of aromatic fibresKaracan, Ismail January 1986 (has links)
No description available.
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Oral hyoglycaemic compounds in Anvillea garcinii.ssp. radiataHaman, M. R. January 1987 (has links)
No description available.
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Conformational interactions involving aromatic ringsHowe, T. J. January 1988 (has links)
No description available.
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Multinuclear magnetic resonance studies on the metabolism model of fluoroaromatic xenobioticsTugnait, Meera January 1994 (has links)
No description available.
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Conformational analysis via LIF spectroscopy of jet cooled molecules : hydroxy- and amino-benzoic acid estersHepworth, Peter January 1993 (has links)
No description available.
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Photochemistry of chlorinated and brominated diaryl ether environmental contaminantsRayne, Sierra. 10 April 2008 (has links)
No description available.
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Circular Dichroism studies on the aromatic residues of fructose 1, 6-Bisphosphatase from Turkey liverOgoe, Samuel A. 01 August 1976 (has links)
This thesis presents a detailed description and analysis of the circular dichroism studies performed on the aromatic residues of fructose 1, 6-bisphosphatase (FbPase) from turkey liver under various experimental conditions. Circular dichroism studies performed on the aromatic residues of FbPase indicate that the presence of the substrate, fructose 1, 6-bisphosphate (FbP) and/or the allosteric inhibitor, adenosine monophosphate (AMP) as well as changes in the pH of the medium produce significant effects on the conformation of the enzyme. The effect of the inhibitor, AMP, on the conformation of the enzyme is more pronounced than that of the substrate, FbP.
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