What Controls the Limit of Supercooling and Superheating of Pinned Ice Surfaces?
Source abstract
Abstract
Cold-adapted organisms produce antifreeze proteins and glycoproteins to control the growth, melting and recrystallization of ice. It has been proposed that these molecules pin the crystal surface, creating a curvature that arrests the growth and melting of the crystal. Here we use thermodynamic modeling and molecular simulations to demonstrate that the curvature of the superheated or supercooled surface depends on the temperature and distances between ice-binding molecules, but not the details of their interactions with ice. We perform simulations of ice pinned with the antifreeze protein TmAFP, polyvinyl alcohol with different degrees of polymerization, and model ice-binding molecules to determine the thermal hystereses on melting and freezing, i.e. the maximum curvature that can be attained before, respectively, ice melts or grows irreversibly over the ice-binding molecules. We find that the thermal hysteresis is controlled by the bulkiness of the ice-binding molecules and their footprint at the ice surface. We elucidate the origin of the asymmetry between freezing and melting hysteresis found in experiments and propose guidelines to design synthetic antifreeze molecules with potent thermal hysteresis activity.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Physiological and biochemical adaptations · nanoparticles nucleation surface interactions · Advanced Thermodynamics and Statistical Mechanics
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemistry, The University of Utah, 315 South 1400 East, Salt Lake City, Utah 84112-0850, United States
Funding
Division of Chemistry
References (74)
Show source-provided references
1. 10.1126/science.163.3871.107310.1126/science.163.3871.1073 ↗
2. 10.1073/pnas.74.6.258910.1073/pnas.74.6.2589 ↗
3. 10.1016/S0006-3495(93)81361-410.1016/S0006-3495(93)81361-4 ↗
4. 10.1016/S0006-3495(91)82234-210.1016/S0006-3495(91)82234-2 ↗
5. 10.1021/acs.chemrev.7b0028510.1021/acs.chemrev.7b00285 ↗
6. 10.1021/cr950260c10.1021/cr950260c ↗
7. Wilson P. · Cryo Letters · 1993 · 14 · 31
8. 10.1039/C6SM02867E10.1039/C6SM02867E ↗
9. 10.1016/j.femsle.2005.02.02210.1016/j.femsle.2005.02.022 ↗
10. 10.1006/cryo.1993.103110.1006/cryo.1993.1031 ↗
11. 10.1016/0167-4838(91)90485-I10.1016/0167-4838(91)90485-I ↗
12. 10.1038/3501863910.1038/35018639 ↗
13. 10.1039/C4RA12638F10.1039/C4RA12638F ↗
14. 10.1038/nbt0997-88710.1038/nbt0997-887 ↗
15. 10.1073/pnas.090945610710.1073/pnas.0909456107 ↗
16. 10.1126/science.245.4917.50510.1126/science.245.4917.505 ↗
17. 10.1073/pnas.090945610710.1073/pnas.0909456107 ↗
18. 10.1016/j.tibs.2014.09.00510.1016/j.tibs.2014.09.005 ↗
19. 10.1006/cryo.1995.100210.1006/cryo.1995.1002 ↗
20. 10.1073/pnas.152410911310.1073/pnas.1524109113 ↗
21. 10.1021/cg500330810.1021/cg5003308 ↗
22. 10.1016/j.cplett.2004.07.02110.1016/j.cplett.2004.07.021 ↗
23. 10.1021/acs.biochem.6b0086410.1021/acs.biochem.6b00864 ↗
24. 10.1016/j.micromeso.2010.08.00110.1016/j.micromeso.2010.08.001 ↗
25. 10.1103/PhysRevE.73.01160810.1103/PhysRevE.73.011608 ↗
26. 10.1021/bm400217j10.1021/bm400217j ↗
27. 10.1021/jp805227c10.1021/jp805227c ↗
28. 10.1021/acs.jpcc.7b1026510.1021/acs.jpcc.7b10265 ↗
29. 10.1021/jacs.6b1221010.1021/jacs.6b12210 ↗
30. Hudait A. · J. Am. Chem. Soc. · 2018
31. 10.1021/acs.jpcc.5b1122110.1021/acs.jpcc.5b11221 ↗
32. 10.1021/jacs.5b0557910.1021/jacs.5b05579 ↗
33. 10.1063/1.489554310.1063/1.4895543 ↗
34. 10.1021/jacs.5b0524210.1021/jacs.5b05242 ↗
35. 10.1021/acs.jpcb.7b1147610.1021/acs.jpcb.7b11476 ↗
36. 10.1021/ja405408n10.1021/ja405408n ↗
37. 10.7554/eLife.0514210.7554/eLife.05142 ↗
38. 10.1016/S0140-7007(01)00045-710.1016/S0140-7007(01)00045-7 ↗
39. 10.1002/cphc.20080061610.1002/cphc.200800616 ↗
40. 10.1039/b010086m10.1039/b010086m ↗
41. 10.1021/jp301240910.1021/jp3012409 ↗
42. 10.1039/b919724a10.1039/b919724a ↗
43. 10.1021/ja210878c10.1021/ja210878c ↗
44. 10.1039/c0py00089b10.1039/c0py00089b ↗
45. 10.1002/cphc.20060053310.1002/cphc.200600533 ↗
46. 10.1021/acs.langmuir.7b0324310.1021/acs.langmuir.7b03243 ↗
47. 10.1063/1.315847010.1063/1.3158470 ↗
48. 10.1039/c1cp22022e10.1039/c1cp22022e ↗
49. 10.1021/jp305468s10.1021/jp305468s ↗
50. 10.1021/ct500487h10.1021/ct500487h ↗
51. 10.1038/nature1058610.1038/nature10586 ↗
52. 10.1021/jp501292810.1021/jp5012928 ↗
53. 10.1063/1.495385410.1063/1.4953854 ↗
54. 10.1021/ja405408n10.1021/ja405408n ↗
55. 10.1021/acs.jctc.6b0029110.1021/acs.jctc.6b00291 ↗
56. 10.1039/C6CP00915H10.1039/C6CP00915H ↗
57. 10.1021/jp101357610.1021/jp1013576 ↗
58. 10.1021/jp511749q10.1021/jp511749q ↗
59. 10.1021/jp303605t10.1021/jp303605t ↗
60. 10.1021/acs.jpclett.7b0185510.1021/acs.jpclett.7b01855 ↗
61. 10.1063/1.489554310.1063/1.4895543 ↗
62. 10.1021/jp411837510.1021/jp4118375 ↗
63. 10.1038/nature2427910.1038/nature24279 ↗
64. 10.1021/ja411507a10.1021/ja411507a ↗
65. 10.1021/jp903439a10.1021/jp903439a ↗
66. 10.1021/ja105144510.1021/ja1051445 ↗
67. 10.1038/nature1058610.1038/nature10586 ↗
68. 10.1021/jp501292810.1021/jp5012928 ↗
69. 10.1021/jacs.7b0954910.1021/jacs.7b09549 ↗
70. 10.1021/jp500039610.1021/jp5000396 ↗
71. 10.1063/1.346296410.1063/1.3462964 ↗
72. 10.1021/cg800269w10.1021/cg800269w ↗
73. 10.1021/jacs.7b1363010.1021/jacs.7b13630 ↗
74. 10.1038/s41467-017-01421-710.1038/s41467-017-01421-7 ↗