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 proteins (AFPs) are grouped together according to similar structure. The one shown on the right is from the winter flounder. | ||
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.<scene name='User:Mary_Ball/AFP/Threonine_residues/3'>See the location of the Threonine Residues</scene> | 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. | ||
<scene name='User:Mary_Ball/AFP/Amino_acids/1'>See the Threonine Residues</scene> | |||
<scene name='User:Mary_Ball/AFP/Threonine_residues/3'>See the location of the Threonine Residues.</scene> | |||
<scene name='User:Mary_Ball/AFP/Amino_acids/1'>See the Threonine Residues.</scene> | |||
<scene name='User:Mary_Ball/Sandbox/Wfb/1'>Go back to the WFB Alpha Helix</scene> | <scene name='User:Mary_Ball/Sandbox/Wfb/1'>Go back to the WFB Alpha Helix.</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 concluded that the "face" with the repeated Threonines promotes binding to ice crystals. | 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. | ||
