User:Mary Ball/AFP: Difference between revisions
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===WINTER FLOUNDER ANTIFREEZE PROTEIN=== | ===WINTER FLOUNDER ANTIFREEZE PROTEIN=== | ||
Type I antifreeze proteins (AFPs) are grouped together according to similar structure. The one shown on the right is from the winter flounder. | |||
Type I antifreeze | |||
This AFP consists of a chain of 37 amino acids that forms a single alpha-helix. Four threonines are evenly spaced in the chain, such that there are three 11-amino-acid repeats. In the single alpha-helix that forms, the threonines all lie on one "face" of the helix. | This AFP consists of a chain of 37 amino acids that forms a single alpha-helix. Four threonines are evenly spaced in the chain, such that there are three 11-amino-acid repeats. In the single alpha-helix that forms, the threonines all lie on one "face" of the helix. | ||
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<scene name='User:Mary_Ball/Sandbox/Amino_acids/1'>Click here to see a labelled Ala.</scene> <scene name='User:Mary_Ball/AFP/Threonine_residues/2'>Scene with Threonine Residues Labelled</scene> | <scene name='User:Mary_Ball/Sandbox/Amino_acids/1'>Click here to see a labelled Ala.</scene> <scene name='User:Mary_Ball/AFP/Threonine_residues/2'>Scene with Threonine Residues Labelled</scene> | ||
Baardsnes, et al (1999) created mutations that reduced the protein's ice-binding ability. They also compared the sequences of five different type I AFP molecules. They | Baardsnes, et al (1999) created mutations that reduced the protein's ice-binding ability. They also compared the sequences of five different type I AFP molecules. They concluded that the "face" with the repeated Threonines promotes binding to ice crystals. | ||
===REFERENCE=== | |||
New ice-binding face for type I antifreeze protein., Baardsnes J, Kondejewski LH, Hodges RS, Chao H, Kay C, Davies PL, FEBS Lett. 1999 Dec 10;463(1-2):87-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10601644 10601644] | |||
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