Ice growth acceleration by antifreeze proteins leads to higher thermal hysteresis activity.

dc.contributor.authorDrori, Ran
dc.contributor.authorDeng, J.
dc.contributor.authorApfelbaum, E.
dc.contributor.orcid0000-0002-6436-5602en_US
dc.date.accessioned2024-02-13T21:18:40Z
dc.date.available2024-02-13T21:18:40Z
dc.date.issued2020
dc.descriptionResearch article / Open accessen_US
dc.description.abstractSince some antifreeze proteins and glycoproteins (AF(G)Ps) cannot directly bind to all ice 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 the 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.en_US
dc.description.sponsorshipAcknowledgments The authors thank Prof. Peter Davies for sharing LpAFP and AFPIII-QAE samples, Dr. Konrad Meister and Prof. Arthur DeVries for sharing the AFGPs and AFPI. The authors also thank Nechama Dembitzer and Nicole Soussana for data collection.en_US
dc.identifier.citationDeng, J., Apfelbaum, E. & Drori, R. (2020). Ice growth acceleration by antifreeze proteins leads to higher thermal hysteresis activity. The Journal of Physical Chemistry B, 124(49), 11081-11088.en_US
dc.identifier.issn1520-5207
dc.identifier.urihttps://pubmed.ncbi.nlm.nih.gov/32472617/en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12202/9811
dc.language.isoen_USen_US
dc.publisherOriginal Publication: Washington, D.C. : American Chemical Society, c1997-en_US
dc.relation.ispartofseriesThe Journal of Physical Chemistry B;124(49)
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectAntifreeze proteinsen_US
dc.subjectIceen_US
dc.subjectAccelerationen_US
dc.subjectAdsorptionen_US
dc.subjectCrystallizationen_US
dc.subjectFreezingen_US
dc.subjectbipyramidal crystalen_US
dc.subjectantifreeze proteins and glycoproteins (AF(G)Ps)en_US
dc.titleIce growth acceleration by antifreeze proteins leads to higher thermal hysteresis activity.en_US
dc.typeArticleen_US
local.yu.facultypagehttps://www.yu.edu/faculty/pages/drori-ranen_US

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