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This 15 page paper provides an overview of the effects of zinc occupancy on human o6-alkylguanine-DNA allkyltranferase. Bibliography lists 12 sources.
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15 pages (~225 words per page)
File: MH11_MHExpZin.rtf
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AGT, as a DNA repair protein. The researchers state that AGT, in particular human AGT (hAGT), protects cells from mutagenic, carcinogenic and apoptopic factors that can negatively impact function
(See Samson, 1992). Unlike a number of the proteins that carry out similar DNA-related functions, AGT is not an enzyme, and so it works to restore DNA through the
"irreversible transfer of adduct substituents to an internal active-site sulfar atom" (Rasimas et al, 2003, p. 980). As a result of increasing interest in the importance of hAGT, two crystal
structures have been studied, published and compared (Rasimas et al, 2003). While these two structures were very similar, there was one major difference: the presence of a bonded zinc
atom. Prior to this comparison and the subsequent discovery of the presence of a bonded zinc atom, no experiments prior to this discovery suggested that hAGT was a metalloprotein
(Rasimas et al, 2003). Prior studies of hAGT, as well as AGT from other mammalian and microbial sources, demonstrate the fact that no metal was present and no metal
was needed for the performance of their function in DNA repair (Rasimas et al, 2003; See also Moore et al, 1994). After assessing data regarding the importance of
transition metals, including zinc, the researchers asserted that the zinc found in the comparative view of hAGT might in fact play a significant role in some DNA repair processes (Rasimas
et al, 2003). The question developed by the researchers, then, was whether zinc present in the comparative analysis of hAGT is a normal, but nonfunctional component of the protein or
whether it plays a key role in the structure and performance of hAGT. The researchers analysis suggests that hAGT is in fact a metalloprotein, and that this metalloprotein is
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