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Ice Growth Acceleration by Antifreeze Proteins Leads to Higher Thermal Hysteresis Activity

preprint
submitted on 04.09.2020 and posted on 04.09.2020 by Jinzi Deng, Elana Apfelbaum, Ran Drori

Since some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all crystal planes, they change ice crystal morphology by minimizing the area of the crystal planes to which they cannot bind until crystal growth is halted. Previous studies found that growth along the c-axis (perpendicular to the basal plane, the crystal plane to which these AF(G)Ps cannot bind) is accelerated by some AF(G)Ps, while growth of other planes is inhibited. The effects of this growth acceleration on crystal morphology and on the thermal hysteresis activity are unknown to date. Understanding these effects will elucidate the mechanism of ice growth inhibition by AF(G)Ps. Using cold stages and an Infrared laser, ice growth velocities and crystal morphologies in AF(G)P solutions were measured. Three types of effects on growth velocity were found: concentration-dependent acceleration, concentration-independent acceleration, and concentration-dependent deceleration. Quantitative crystal morphology measurements in AF(G)P solutions demonstrated that adsorption rate of the proteins to ice plays a major role in determining the morphology of the bipyramidal crystal. These results demonstrate that faster adsorption rates generate bipyramidal crystals with diminished basal surfaces at higher temperatures compared to slower adsorption rates. The acceleration of growth along the c-axis generates crystals with smaller basal surfaces at higher temperatures leading to increased growth inhibition of the entire crystal.

History

Email Address of Submitting Author

rdrori@yu.edu

Institution

Yeshiva University

Country

United States

ORCID For Submitting Author

0000-0002-6436-5602

Declaration of Conflict of Interest

No conflict of interest

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