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Full-Text Articles in Physical Sciences and Mathematics
The Synthesis And Characterization Of Some Thermally Stable Polypyrazoles And Acetylene Terminated Aspartimides, John W. Connell
The Synthesis And Characterization Of Some Thermally Stable Polypyrazoles And Acetylene Terminated Aspartimides, John W. Connell
Theses and Dissertations
Reactions involving the nucleophilic addition cyclization to activated acetylenes have been employed as a novel route to moderate to high molecular weight polymers. Polypyrazoles (PI to P12) have been prepared from the Michael-type addition cyclization of various aromatic dihydrazines to aromatic dipropynones in m-cresol. The aromatic dihydrazines employed were 4, 4'-dihydrazinodiphenyl ether (4,4' -DHDPE), 4,4 '-dihydrazinodiphenylmethane (4, 4'-DHDPM), and 4, 4' -dihydrazinodiphenyl sulfone (4,4'-DHDPS). The dipropynone sutilized were 1,1’- (1,4-phenylene) bis (3-phenyl- 2-propyn-l-one), (l,4 -PPPO), 1,1’ - (1, 3-phenylene) bis (3 -phenyl- 2 -propyn-l-one), (1,3-PPPO), 1,1 '-(1,4 -phenylene) bis (2 -propyn- l-one), (1,4 -PPO), and 1,1’- (1,3 -phenylene) bis (2 …
Electrochemical Investigation Of The Effects Of Temperature, Ph, And Electrolyte On The Electron Transfer Reactions Of Cytochrome C, Kent Brian Koller
Electrochemical Investigation Of The Effects Of Temperature, Ph, And Electrolyte On The Electron Transfer Reactions Of Cytochrome C, Kent Brian Koller
Theses and Dissertations
Spectroelectrochemical and electrochemical methods have been used to investigate the characteristics of heterogeneous electron transfer between cytochrome c and indium oxide electrodes. Direct electron transfer between cytochrome c and solid electrodes is of interest due to the interfacial character of electron transfer between the protein and its membrane-bound physiological redox partners. The conformation of ferricytochrome c is affected more by changes in temperature or pH than is its reduced form, ferrocytochrome c. This difference in conformational stability is attributed to the +1 charge of the heme in ferricytochrome c that is largely embedded in the hydrophobic interior of the enzyme. …