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http://hdl.handle.net/11375/7005
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DC Field | Value | Language |
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dc.contributor.advisor | Yang, Daniel S.C. | en_US |
dc.contributor.author | Sicheri, Frank | en_US |
dc.date.accessioned | 2014-06-18T16:37:47Z | - |
dc.date.available | 2014-06-18T16:37:47Z | - |
dc.date.created | 2010-06-24 | en_US |
dc.date.issued | 1995-07 | en_US |
dc.identifier.other | opendissertations/2305 | en_US |
dc.identifier.other | 3249 | en_US |
dc.identifier.other | 1370466 | en_US |
dc.identifier.uri | http://hdl.handle.net/11375/7005 | - |
dc.description.abstract | <p>The 1.5Å x-ray crystal structure of a lone α-helical antifreeze protein (AFP) from winter flounder is presented, providing the first detailed look at an AFP and its ice binding features. The structure was determined using a non conventional multi-parameter molecular replacement scheme with two idealized α-helices as the search models. The described method may prove useful for the determination of other α-helical structures. The AFP's ice binding structure consists of four repeated ice binding motifs (IBMs), the side chains of which are inherently rigid or restrained by pair-wise side chain interactions to form a flat binding surface. Comparison shows that analogous IBM sequences are found highly conserved in all members of the α-helical class of AFPs. Also revealed are the presence of elaborate N- and C-terminal cap structures which help to account for the AFP's unusual stability for a lone a-helix in aqueous solution. Based on the crystal structure, a model amenable to testing is proposed which accounts for the proteins ice binding ability and specificity. Experiments to test the validity and generality of this ice binding model are proposed.</p> | en_US |
dc.subject | Biochemistry | en_US |
dc.subject | Biochemistry | en_US |
dc.title | Ice Binding Structure and Mechanism of an Antifreeze Protein from Winter Flounder | en_US |
dc.type | thesis | en_US |
dc.contributor.department | Biochemistry | en_US |
dc.description.degree | Doctor of Philosophy (PhD) | en_US |
Appears in Collections: | Open Access Dissertations and Theses |
Files in This Item:
File | Size | Format | |
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fulltext.pdf | 2.36 MB | Adobe PDF | View/Open |
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