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| - | <Structure load='3p4g' size='350' frame='true' align='right' caption=' | + | <Structure load='3p4g' size='350' frame='true' align='right' caption='Fragment of beta-helical antifreeze protein (PDB code [[3p4g]])' scene='Insert optional scene name here' /> |
[[Image:IceBind 1.png |thumb|400px| The ice formation of water (red spheres) being scrambled (blue spheres) by the protein]] | [[Image:IceBind 1.png |thumb|400px| The ice formation of water (red spheres) being scrambled (blue spheres) by the protein]] | ||
[[Image:IceBind 2.png |thumb|400px| Threonines and Aspartates are lined up in a manner that binds nearby water molecules in a manner that is off-set from the ice crystal lattice]] | [[Image:IceBind 2.png |thumb|400px| Threonines and Aspartates are lined up in a manner that binds nearby water molecules in a manner that is off-set from the ice crystal lattice]] | ||
Revision as of 08:50, 12 January 2026
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Marinomonas primoryensis
Isolated from marine coastal sea-ice. Marinomonas primoryensis is aerobic, Gram-negative, psychrophilic, halophilic and motile by means of a single polar flagellum. This bacteria survives in extreme cold and high salinity environments.
Structural highlights
The distinct beta-sheet roll in this ice binding protein is stabilized by a series of . This beta sheet roll sets up in a row several amino acids capable of forming a hydrogen bond with water creating a
References
Garnham, Christopher P., Robert L. Campbell, and Peter L. Davies. "Anchored clathrate waters bind antifreeze proteins to ice." Proceedings of the National Academy of Sciences 108.18 (2011): 7363-7367.
