Why be moral? One possible, and compelling answer is that to act morally is in an agent's self-interest. Such an answer can be either elevationist (broadly speaking the Aristotelian/Platonic approach) where self-interest is elevated to coincide with living the good life, or reductionist where morality is defined as acting in an agent's self-interest. Elevationist moral theories appear flawed. If you are in possession of information that, if divulged, will bring about the deaths of others then it may be virtuous to stay silent. However, if staying silent results in you being slowly tortured to death in an effort to extract the information then it seems bizarre to suggest that in doing so you are flourishing, happy, or acting out of self-interest. Reductionist moral theories, acting for the 'good of self' rather than the 'good of others', are widely considered to be the antithesis of morality. Moral philosophers tend to attack such positions claiming that the doctrine of egoism is unworkable. It is commonly claimed that any theory which recommends 'an agent do x if x is in the agent's best interest' is inconsistent, incoherent, or contradictory and fails to meet the basic requirements of a moral theory (notably the requirement of universalisability). I begin this thesis with an examination of ethical egoism in its most widely known consequentialist form; i.e. an agent ought to act so as to bring about the best consequences for that agent. I examine the major criticisms of this theory and demonstrate that the axioms of egoism can be developed so as to overcome these criticisms. I argue that consequentialist based ethical egoism is coherent, consistent and noncontradictory. However, I go on to argue that while egoism can be formulated in a manner that overcomes all the aforementioned analytic criticisms it is a flawed moral theory in that within certain contexts the action deemed morally correct by egoism is, as a matter of fact, morally pernicious. That a theory contains a flaw is not reason enough to discard the entire theory and I go on to contend that the problem with egoism is the consequentialist approach, not the fact that it is based on self-interest. In Part 2 of the thesis I abandon the consequentialist approach and examine the possibility of a flourishing-based form of ethical egoism. I further develop the axioms of egoism established in Part 1 through an examination of the concept of flourishing (as commonly associated with virtue ethics). Ultimately I tread a path between the consequentialist and elevationist positions. While I do not elevate self-interest to acting virtuously I do contend that an egoist must adopt certain virtues if that egoist is to have the best possibility to flourish. However, I further contend that an egoist ought to act so as to promote that which the egoist values and that this agent-relative hierarchy of values, which necessarily contains certain virtues, determines the manner in which an egoist ought to act.

<p>Hedgehog related genes have been shown to play a major role in development in all deuterostomes. In C.elegans, such genes have been found where the similarity is restricted to the C-terminal domain. This work has focused on the hedgehog related C.elegans proteins called ground (grd), ground-like (grl), and wart (wrt) which appear to form a unique structural family.These proteins are cysteine rich and have conserved cysteine patterns which, together with thethought that they are secreted, are expected to be in disulfide form. Since the extracellular environment is very oxidizing and due to the conserved cysteine pattern, disulfide bonds are thought to play a big part in the folding and stabilization of these proteins. The stability of the protein and the formation of a disulfide bond are related through a thermodynamic cycle, which insures that the stabilization of the protein by the disulfide is reflected by the identical stabilization of the disulfide by the protein. Practically, there are numerous parameters that can be used to try to achieve the correct disulfide bonds and folding, when doing in vitro trials, some of which were used in this project. C.elegans proteins grd-5, grd-13, grl-24, wrt-3 and wrt-5 were studied in this project. All of the proteins were expressed and purified with success, with theexception of grl-24. All constructs formed inclusion bodies. Some refolding attempts were performed on grd-13 and wrt-3. The presence of a disulfide bond in refolded grd-13 was demonstrated using chemical fragmentation. In general, these attempts did not give correctly folded proteins but provide a foundation to continue experiments aimed at producing a native-like protein for structural and functional studies.</p>

Hedgehog related genes have been shown to play a major role in development in all deuterostomes. In C.elegans, such genes have been found where the similarity is restricted to the C-terminal domain. This work has focused on the hedgehog related C.elegans proteins called ground (grd), ground-like (grl), and wart (wrt) which appear to form a unique structural family.These proteins are cysteine rich and have conserved cysteine patterns which, together with thethought that they are secreted, are expected to be in disulfide form. Since the extracellular environment is very oxidizing and due to the conserved cysteine pattern, disulfide bonds are thought to play a big part in the folding and stabilization of these proteins. The stability of the protein and the formation of a disulfide bond are related through a thermodynamic cycle, which insures that the stabilization of the protein by the disulfide is reflected by the identical stabilization of the disulfide by the protein. Practically, there are numerous parameters that can be used to try to achieve the correct disulfide bonds and folding, when doing in vitro trials, some of which were used in this project. C.elegans proteins grd-5, grd-13, grl-24, wrt-3 and wrt-5 were studied in this project. All of the proteins were expressed and purified with success, with theexception of grl-24. All constructs formed inclusion bodies. Some refolding attempts were performed on grd-13 and wrt-3. The presence of a disulfide bond in refolded grd-13 was demonstrated using chemical fragmentation. In general, these attempts did not give correctly folded proteins but provide a foundation to continue experiments aimed at producing a native-like protein for structural and functional studies.