Winter Flounder "Antifreeze" Proteins: Synthesis and Ice Growth Inhibition of Analogs that Probe the Relative Importance of Hydrophobic and Hydrogen-Bonding Interactions
Two series of mutant polypeptides of the type I, 37-residue winter flounder 'antifreeze' protein have been synthesized and analyzed by nanoliter osmometry, the 'ice hemisphere' test, measurement of ice growth hysteresis and circular dichroism (CD) spectroscopy. In series 1 peptides the central two threonines and all four threonines of the native protein were mutated to serine. In series 2 peptides two additional salt bridges (K7, E11 and K29, E33) were incorporated, and all four threonine...[Show more]
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|Source:||Journal of the American Chemical Society|
|01_Haymet_Winter_Flounder_"Antifreeze"_1999.pdf||153.63 kB||Adobe PDF||Request a copy|
|02_Haymet_Winter_Flounder_"Antifreeze"_1999.pdf||149.87 kB||Adobe PDF||Request a copy|
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