Thesis (D. Min.)--Bethel Theological Seminary, 1993. / Includes bibliographical references (leaves 143-153).

Thesis (D. Miss.)--Trinity Evangelical Divinity School, 1988. / Abstract. Includes bibliographical references (leaves 288-300).

Thesis (D. Miss.)--Trinity Evangelical Divinity School, 1988. / Abstract. Includes bibliographical references (leaves 288-300).

Thesis (M.A.)--Western Conservative Baptist Seminary, 1984. / Includes bibliographical references (leaves 74-80).

No description available.

The structure of the dihydrolipoamide acetyltransferase (E2p) component of the pyruvate dehydrogenase complex from <i>Escherichia coli</i> and its role in catalysis were studied by the combined approaches of protein engineering, limited proteolysis and <SUP>1</SUP>H-n.m.r. spectroscopy. Genetic reconstruction of the E2p component (performed elsewhere) produced a series of mutant complexes assembled around E2p chains which contain only a single lipoyl domain and an associated (alanine+proline)-rich linker region of gradually diminishing lengths (32, 20, 13, 7 and 1 residue(s), respectively, in the pGS110-,pGS156-,pGS186 ,pGS187- and pGS188-encoded complexes). When this region was shortened to 13 residues or less, the system of active-site coupling in the enzyme complex was dramatically impaired, although the individual enzyme activities were unaffected. The role of the (alanine+proline)-rich region in facilitating moment of the lipoyl domains in catalysis was thus established. The (alanine+proline)-rich regions of the wild-type E2p chains had previously been conjectured to be the source of the unexpectedly sharp resonances in the <SUP>1</SUP>H-n.m.r. spectrum of the enzyme complex, and hence to be conformationally mobile. Examination of the genetically restructured complexes by <SUP>1</SUP>H-n.m.r. spectroscopy revealed that the intensity of the sharp peaks in the spectra correlated well with the length of the (alanine+proline)-rich region in each complex. Furthermore, resonances from a single histidine residue engineered into the (alanine+proline)-rich region of a pGS110-encoded E2p chain was clearly visible in the <SUP>1</SUP>H-n.m.r. spectrum of the resulting enzyme complex. These experiments proved unequivocally that the (alanine+proline)-rich regions are conformationally mobile. The <SUP>1</SUP>H-n.m.r. spectra of the mutant complexes with the most severe deletions in the E2p chains differed from those of the wild-type and pGS110-encoded complexes in that they displayed a novel sharp peak which was not initially apparent in the spectra of the parent assemblies. This resonance was tentatively assigned to another, shorter (alanine+proline)-rich sequence in the E2p chain, which separates the dihydrolipoamide dehydrogenase (E3)-binding and inner-core domains in the <i>C</i>-terminal half of the molecule. It is likely therefore that this sequence is also conformationally flexible. Antibodies against a synthetic peptide with the sequence of the long (alanine+proline)-rich region of the pGS110-encoded E2p chain were raised elsewhere. Binding of the Fab fragments of these antibodies to the pGS110-encoded complex was found to inhibit the overall complex activity even though the activities of the three component enzymes were not affected. Antibody binding was shown to prevent both the reductive acetylation of the lipoyl domains at the pyruvate decarboxylase (E1p) active site and the transfer of acetyl groups between adjacent lipoyl domains, demonstrating the role of the (alanine+proline)-rich sequence in the mechanism of substrate transfer between active sites. A detailed study of the conformation of the (alanine+proline)-rich regions was also undertaken. Synthetic peptides were obtained with sequences identical to the central and innermost such regions of the wild-type E2p chain. The conformation of these peptides in aqueous solution was studied by circular dichroism, <SUP>1</SUP>H-n.m.r. and <SUP>13</SUP>C-n.m.r. spectroscopy. Relaxation time and nOe data pointed to an extended conformation for the peptides, a structure enforced by the predominantly <i>trans</i> Ala-Pro peptide bond. The functional consequences of this conformation and the role of these sequences in the structure and the function of the enzyme complex are discussed.

Thesis (M.A.)--Trinity Evangelical Divinity School, 1991. / Abstract. Includes bibliographical references (leaves 175-187).

This thesis, which moves through three stages, asks whether the compulsory provision of a daily act of collective worship can be justified in the schools of a liberal society. It begins with an analysis of the public debate which has surrounded its presence since legislation in 1944 formalised existing practice, and notes that its arguments are based on differing perceptions of the value of religious practice, the needs of the child, the relationship between religion and morality, and the nature of society. Because this public debate is often distanced from actual practice, research was undertaken in primary and secondary schools in England and Wales and is described in the central section of the study. The methods used to gather data are first discussed and are then followed by reports on the information acquired by means of a national questionnaire, as well as observation and interviews which were carried out with teachers and pupils in the south west of England and a city in the Midlands. The findings show that the legal requirements are met in the majority of primary schools, but that pupils' transfer to the secondary school frequently marks a point of transition from daily worship to a weekly assembly, except in the voluntary sector. Adult respondents discuss their attitudes to collective worship, the obstacles they encounter in meeting the legal requirements and the approaches adopted in their schools. The most important features of collective worship are perceived by teachers and pupils to be the contribution it makes to the development of a sense of community, the celebration of achievement and the ethos of the school. Conversations with pupils reveal the changes in belief which occur as they mature, and shed further light on provision in schools, reflecting young people's declining willingness to participate in religious worship. The evidence of the data reveals that opposition to collective worship is expressed by young people and their teachers in the language of individualism and choice. The philosophical analysis of the concluding section therefore examines the question of the justifiability of collective worship from a liberal perspective, giving particular attention to questions of autonomy, rights, indoctrination and the distinction between the public and private domains. Recognising, howevcr, that communitarianism provides a major challenge to liberalism, a study is also made of relevant arguments from this perspective before concluding that collective worship cannot be justified from either position. Nevertheless, schools claim that they intend to maintain the provision of assembly in a maimer which meets their needs, and the conclusion suggests that the way ahead may be to build on the current strengths of provision and to replace the traditional elements of participatory worship with a programme which develops a deeper emphasis on the spiritual and cultural dimensions of experience.

No description available.

Thesis (D. Min.)--Western Conservative Baptist Seminary, 1990. / Abstract. Includes bibliographical references (leaves 521-528).