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A histochemical method for the localization of choline acetyltransferase, the synthesizing enzyme of acetylcholine has been recently developed. Conditions of the method were first investigated and optimized in the spinal cord of the rat where cholinergic neurones are known to be present. Following standardization of the method the localization of the enzyme was studied in the deep cerebellar nuclei. A series of transverse sections were stained to facilitate, allocation of cells demonstrating enzyme activity to their respective nuclei as described in the literature. The presence of choline acetyltransferase was used as a direct indication of a cholinergic neurone, and was found predominantly in the cells in the ventral portion of the lateral nucleus, on the border of the interpositus and lateral nuclei and in the caudal portion of the medial nucleus. The results obtained are consistent with other studies indicating that a portion of the cerebello-thalamic pathway is cholinergic. / Medicine, Faculty of / Cellular and Physiological Sciences, Department of / Graduate

It is well known that information contained in a protein sequence is what allows it to fold into its three-dimensional shape, which performs a specific function. It has been possible for some time to search for proteins with similar sequences, using bioinformatics tools such as BLAST. But it is also known that proteins with similar, or even the same sequence can adopt different structures and vice-versa. With this in mind, we look to use a method called Rosetta-HMMER to perform conformationally specific sequence searches in order to exploit this property of proteins. This method involves the use of Rosetta to redesign protein structures to fit a specified α-carbon backbone, and then uses HMMER to generate a sequence profile. This profile can then be used to query for sequences able to adopt the specified backbone structure. These collected sequences can then be aligned for the purpose of performing statistical coupling analysis. We have used this Rosetta-HMMER method in conjunction with available structures of the α7 acetylcholine receptor to show that distinct sequence profiles generated from different conformations of the same protein are capable of retrieving unique sets of natural sequences when used as a query. We have also shown that when these unique sets of natural sequences are used to perform statistical coupling analysis, different residues are identified as statistically coupled, potentially generating insight into residues that have more potential importance for one backbone conformation over another.

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Thesis (M.Sc.)--Memorial University of Newfoundland, 2004. / Restricted until October 2005. Bibliography: leaves 71-94.

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