Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide
The melting of pure ice single crystals can be inhibited by the presence of an antifreeze glycopeptide isolated from an Antarctic fish. This inhibition effect exhibits crystallographic dependence and can result in superheating of the crystal by heat conduction across the ice-solution interface. The...
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Language: | English |
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American Association for the Advancement of Science (AAAS)
1989
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Online Access: | http://dx.doi.org/10.1126/science.245.4917.505 https://www.science.org/doi/pdf/10.1126/science.245.4917.505 |
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craaas:10.1126/science.245.4917.505 2024-06-23T07:45:51+00:00 Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide Knight, C. A. DeVries, A. L. 1989 http://dx.doi.org/10.1126/science.245.4917.505 https://www.science.org/doi/pdf/10.1126/science.245.4917.505 en eng American Association for the Advancement of Science (AAAS) Science volume 245, issue 4917, page 505-507 ISSN 0036-8075 1095-9203 journal-article 1989 craaas https://doi.org/10.1126/science.245.4917.505 2024-06-06T04:00:54Z The melting of pure ice single crystals can be inhibited by the presence of an antifreeze glycopeptide isolated from an Antarctic fish. This inhibition effect exhibits crystallographic dependence and can result in superheating of the crystal by heat conduction across the ice-solution interface. The antifreeze molecules inhibit melting in a manner more or less symmetrical to their well-known effect of inhibiting freezing. The melting effect is best expressed at concave ice interfaces, whereas the freezing effect is best expressed at convex ones. Both are restricted to orientations near (101̅0) with the particular antifreeze that was used. Article in Journal/Newspaper Antarc* Antarctic AAAS Resource Center (American Association for the Advancement of Science) Antarctic Science 245 4917 505 507 |
institution |
Open Polar |
collection |
AAAS Resource Center (American Association for the Advancement of Science) |
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craaas |
language |
English |
description |
The melting of pure ice single crystals can be inhibited by the presence of an antifreeze glycopeptide isolated from an Antarctic fish. This inhibition effect exhibits crystallographic dependence and can result in superheating of the crystal by heat conduction across the ice-solution interface. The antifreeze molecules inhibit melting in a manner more or less symmetrical to their well-known effect of inhibiting freezing. The melting effect is best expressed at concave ice interfaces, whereas the freezing effect is best expressed at convex ones. Both are restricted to orientations near (101̅0) with the particular antifreeze that was used. |
format |
Article in Journal/Newspaper |
author |
Knight, C. A. DeVries, A. L. |
spellingShingle |
Knight, C. A. DeVries, A. L. Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
author_facet |
Knight, C. A. DeVries, A. L. |
author_sort |
Knight, C. A. |
title |
Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
title_short |
Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
title_full |
Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
title_fullStr |
Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
title_full_unstemmed |
Melting Inhibition and Superheating of Ice by an Antifreeze Glycopeptide |
title_sort |
melting inhibition and superheating of ice by an antifreeze glycopeptide |
publisher |
American Association for the Advancement of Science (AAAS) |
publishDate |
1989 |
url |
http://dx.doi.org/10.1126/science.245.4917.505 https://www.science.org/doi/pdf/10.1126/science.245.4917.505 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Science volume 245, issue 4917, page 505-507 ISSN 0036-8075 1095-9203 |
op_doi |
https://doi.org/10.1126/science.245.4917.505 |
container_title |
Science |
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245 |
container_issue |
4917 |
container_start_page |
505 |
op_container_end_page |
507 |
_version_ |
1802642695527596032 |