Ocean Eel Pout

We next applied the implicit solvent simulation method to study the stability of a globular protein from ocean eel pout. Table 3 summarizes the parameters use in both an explicit water simulation and an implicit water simulation. 

We have systematically analyzed four different antifreeze proteins and their interactions with various planes of ice as well as studied their behavior in water. We have also presented our initial efforts on the dynamics of an antifreeze protein at the ice/water interface. Additionally we have discussed the 

Color versions of all the figures in this chapter can be obtained from the following web site  

We would like to thank all of the students involved in this work, especially Mark Taylor, Richard Maughon, and Chris Salmon. We especially would like to thank our close collaborators Charles Knight and Frank Sonnischen for their assistance, kind comments and suggestions throughout. This work has been funded by the National Science Foundation MCB-9322602 and MCB-9723271. 

flrrutia. and D. Tursman, Thermal hysteresis proteins, in Advances in Low Temperature Biology, JAl Press Ltd., 1993, 131. 

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Figure 9. Ribbon representation of the ocean eel pout Type III antifreeze protein. The N-face is parallel to the figure caption, the C-face is at the 1 o clock position, and the two-strand region is at the 10 o clock position.

Figure 18. Summary of the analyses comparing the explicit solvent with the implicit solvent simulations on the Type III antifreeze protein, ocean eel pout. The top left graph compares the potential energy as a function of simulation time for the two simulations. The top right graph compares the RMS deviation of the antifreeze protein structure as a function of time. The bottom graph is a plot of the radius of gyration versus simulation time for the two simulations.

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