Thermal hysteresis: Difference between revisions
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'''Thermal [[hysteresis]]''' is used in reference to a difference between [[freezing|freezing temperature]] and [[melting point|melting temperature]], as is the condition for pure water, which melts at close to 0°C, but will supercool to −40°C when no [[nucleation|nucleators]] are present<ref>{{cite book | coauthors = Richard E. Lee, Jr., Gareth J. Warren, L.V. Gusta (Editors) | title = Biological Ice Nucleation and Its Applications | publisher = APS PRESS (The American Phytopathological Society) | date = 1995 | location = St. Paul, Minnesota | pages = 1-28 | url = http://www.shopapspress.org/41728.html |isbn = 0890541728}}</ref>. When nucleators are present (such as bacterial nucleating [[protein]]s) the melting point and the frrezing point of water are nearly the same, and there is no thermal hystersis<ref>{{cite book | coauthors = Richard E. Lee, Jr., Gareth J. Warren, L.V. Gusta (Editors) | title = Biological Ice Nucleation and Its Applications | publisher = APS PRESS (The American Phytopathological Society) | date = 1995 | location = St. Paul, Minnesota | pages = 204 | url = http://www.shopapspress.org/41728.html |isbn = 0890541728}}</ref>.. When nucleators are present with [[antifreeze protein]]s, the freezing point is depressed below the melting point, restoring thermal hysteresis. | '''Thermal [[hysteresis]]''' is used in reference to a difference between [[freezing|freezing temperature]] and [[melting point|melting temperature]], as is the condition for pure water, which melts at close to 0°C, but will supercool to −40°C when no [[nucleation|nucleators]] are present<ref>{{cite book | coauthors = Richard E. Lee, Jr., Gareth J. Warren, L.V. Gusta (Editors) | title = Biological Ice Nucleation and Its Applications | publisher = APS PRESS (The American Phytopathological Society) | date = 1995 | location = St. Paul, Minnesota | pages = 1-28 | url = http://www.shopapspress.org/41728.html |isbn = 0890541728}}</ref>. When nucleators are present (such as bacterial nucleating [[protein]]s) the melting point and the frrezing point of water are nearly the same, and there is no thermal hystersis<ref>{{cite book | coauthors = Richard E. Lee, Jr., Gareth J. Warren, L.V. Gusta (Editors) | title = Biological Ice Nucleation and Its Applications | publisher = APS PRESS (The American Phytopathological Society) | date = 1995 | location = St. Paul, Minnesota | pages = 204 | url = http://www.shopapspress.org/41728.html |isbn = 0890541728}}</ref>.. When nucleators are present with [[antifreeze protein]]s, the freezing point is depressed below the melting point, restoring thermal hysteresis. | ||
Revision as of 12:12, 7 May 2008
Thermal hysteresis is used in reference to a difference between freezing temperature and melting temperature, as is the condition for pure water, which melts at close to 0°C, but will supercool to −40°C when no nucleators are present[1]. When nucleators are present (such as bacterial nucleating proteins) the melting point and the frrezing point of water are nearly the same, and there is no thermal hystersis[2].. When nucleators are present with antifreeze proteins, the freezing point is depressed below the melting point, restoring thermal hysteresis.
More precisely, thermal hysteresis describes the condition where thermal history determines the behavior and properties of the system, as happens between the freezing temperature and melting temperature of water, when the temperatures are different. Warming between the two temperatures and cooling between the two temperatures will have different effects, depending on the thermal history, rather than simply on the temperature.
See also
References
- ↑ (1995) Biological Ice Nucleation and Its Applications. St. Paul, Minnesota: APS PRESS (The American Phytopathological Society), 1-28. ISBN 0890541728.
- ↑ (1995) Biological Ice Nucleation and Its Applications. St. Paul, Minnesota: APS PRESS (The American Phytopathological Society), 204. ISBN 0890541728.