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This thesis examines Toni Morrison's fiction and how a complex relationship between love and anger forms the centre of each narrative. This centre is identified as an ambivalent black feminist space in which angry motherlove takes shape. The ambivalent thoughts and actions of African-American mothers, in Beloved, Song of Solomon, The Bluest Eye, Sula, Paradise, Jazz, and Love, gain clarity only when they are reassessed in relation to Morrison's black feminist standpoint. Here, 'New Seeing' is required of Morrison's reader so as to recognise anger as enabling each mother's black feminist protest; she is demanding both her right to be a mother and to be an autonomous self. A uniquely formed angry motherlove represents black women empowered by the knowledge that in loving another they must never deprive themselves of self-love. Black feminist anger also works to oppose the patriarchal anger that is favoured by black men in a post-emancipation era. Hence, there shall also be consideration of how patriarchal anger affects black fatherlove. The thesis is divided into four chapters that look at motherlove in different situations. Chapter One explores black mothering in slavery and how it is protected using angry motherlove. Subsequent chapters will identify how this oppressive regime has continued to impact upon the lives of African-Americans in a post-emancipation era, with the power to distort their expressions of love and anger. Chapter Two investigates how black feminist anger offers a defence against black patriarchal anger in nuclear family homes. Angry love exists in these marital relationships that go on to produce angry motherlove and angry fatherlove. Chapter Three analyses motherlove in relation to self-love within black matriarchies. Chapter Four reflects upon Morrison's changing perspective in her later fiction; she now focuses on forms of 'otherlove' and there is the suggestion that the time for anger has passed.

Although integral membrane proteins represent nearly a quarter of the genes present in both prokaryotes and eukaryotes, progress in this area of research is often hindered due to the nature of their hydrophobic environment. Elucidating the folding pathway of these proteins is essential to understand many membrane mediated biological processes such as signal transduction, ion transport and chemotaxis. The wealth of structural and genetic information on bacteriorhodpsin renders it an ideal model system for the study of membrane proteins. Detailed studies however, necessitate efficient methods for its overexpression and purification. Previous expression systems have reported difficulty in obtaining good yields and simple purification procedures. This thesis investigates a variety of alternative expression and purification systems for the bacterio-opsin gene in Escherichia coli. With sufficient protein, site directed mutagenesis is performed to mutate three proline residues present in the membranous region of bacteriorhodopsin to alanine. The folding kinetics of these mutants is investigated using stopped flow fluorimetry to determine whether proline isomerisation is responsible for a slow step in the folding pathway of bacteriorhodopsin. Comparison of the results with those of the folding kinetics of wild type showed proline isomerisation not to be responsible for the slow step in the pathway. More recent studies have suggested that the slow step may be due to refolding conditions and lateral pressure the lipids impose upon the protein as well as pH. Separate structural studies using mass spectrometry aimed to study the rates of isotopic exchange of amide and side chain protons in bacteriorhodopsin. Low resolution results obtained using matrix assisted laser desorption ionisation mass spectrometry (MALDI-MS) prompted the investigation of electrospray ionisation mass spectrometry (ESI-MS). Techniques for sample preparation were optimised by investigating a variety of solvent systems and initial deuteration experiments performed.