1wfb: Difference between revisions

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[[Image:1wfb.~~jpg~~|left|200px]]

[[Image:1wfb.png|left|200px]]

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~~'''~~WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C~~'''~~

===WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C===

~~==Overview==~~

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~~Antifreeze proteins provide fish with protection against~~ the ~~freezing effect of polar environments by binding~~ to ~~ice surfaces and inhibiting growth of ice crystals. We present~~ the ~~X-ray crystal structure~~ at 1.~~5 A resolution of a lone alpha-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding features~~. ~~These consist of four repeated ice-binding motifs~~, the ~~side chains of which are inherently rigid or restrained by pair-wise side-chain interactions to form a flat binding surface~~. ~~Elaborate amino~~- ~~and carboxy~~-terminal cap structures are also present, which explain the protein's rich alpha-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the <0112> axes of the (2021) ice planes.

The line below this paragraph, {{ABSTRACT_PUBMED_7760940}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7760940 is the PubMed ID number.

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==About this Structure==

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[[Category: Ice binding protein]]

[[Category: Thermal hysteresis protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 13~~:34:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:30:27 2008''

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-[[Image:1wfb.jpg|left|200px]]
+{{Seed}}
+[[Image:1wfb.png|left|200px]]
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 {{STRUCTURE_1wfb|  PDB=1wfb  |  SCENE=  }}
-'''WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C'''
+===WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT-180 DEGREES C===
-==Overview==
+<!--
-Antifreeze proteins provide fish with protection against the freezing effect of polar environments by binding to ice surfaces and inhibiting growth of ice crystals. We present the X-ray crystal structure at 1.5 A resolution of a lone alpha-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pair-wise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap structures are also present, which explain the protein's rich alpha-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the &lt;0112&gt; axes of the (2021) ice planes.
+The line below this paragraph, {{ABSTRACT_PUBMED_7760940}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7760940 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7760940}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Ice binding protein]]
 [[Category: Thermal hysteresis protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:34:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:30:27 2008''