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DNA base interactions with proteins, water, and cations.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
DNA base interactions with proteins, water, and cations.
作者:
Maki, Angele Suzanne.
面頁冊數:
230 p.
附註:
Adviser: Eric T. Kool.
附註:
Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4337.
Contained By:
Dissertation Abstracts International64-09B.
標題:
Chemistry, Biochemistry.
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104276
ISBN:
0496518445
DNA base interactions with proteins, water, and cations.
Maki, Angele Suzanne.
DNA base interactions with proteins, water, and cations.
[electronic resource] - 230 p.
Adviser: Eric T. Kool.
Thesis (Ph.D.)--Stanford University, 2003.
This thesis describes research on three separate projects. In the first project, single-stranded DNA circles that were selected by in vitro selection techniques were characterized. More specifically, elements of their sequences and secondary structure were explored in relation to the ability of the circle to be a good template for the T7 and E. coli RNA polymerases. The results of this study suggest that the secondary structure is very important for template ability and that canonical promoters do not work well in a single-stranded circular DNA context. Moreover, in vitro selection may be the best way to obtain single-stranded circular DNA templates for a given application. In the second project, natural DNA aptamers and DNA aptamers containing a nonnatural nucleotide were characterized. Through determination of their binding affinities using fluorescence polarization, it was found that the aptamers bound nonspecifically to the protein target. Because binding was nonspecific, the effect of nonnatural nucleotide incorporation on the aptamer properties could not be assessed. However, several lessons were learned regarding the approach used to generate the aptamers. Finally, in the third study the mechanism of A-tract DNA curvature was explored using two nucleotide analogs and gel mobility method to quantify DNA curvature. The results suggested that there are two distinct sites in the minor groove where electrostatic interactions contribute to the curvature mechanism. At one site, the interaction is primarily with the T strand, while the interaction is primarily with the A stand at the other site. The results also suggested that major-groove bifurcated hydrogen bonds and junction effects do not play an important role in the mechanism of A-tract curvature.
ISBN: 0496518445Subjects--Topical Terms:
226900
Chemistry, Biochemistry.
DNA base interactions with proteins, water, and cations.
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