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http://hdl.handle.net/11375/7005
Title: | Ice Binding Structure and Mechanism of an Antifreeze Protein from Winter Flounder |
Authors: | Sicheri, Frank |
Advisor: | Yang, Daniel S.C. |
Department: | Biochemistry |
Keywords: | Biochemistry;Biochemistry |
Publication Date: | Jul-1995 |
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> |
URI: | http://hdl.handle.net/11375/7005 |
Identifier: | opendissertations/2305 3249 1370466 |
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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