期刊
JOURNAL OF THE ROYAL SOCIETY INTERFACE
卷 9, 期 77, 页码 3249-3259出版社
ROYAL SOC
DOI: 10.1098/rsif.2012.0388
关键词
ice-binding proteins; melting shapes; ice-structuring proteins; crystal growth; antifreeze proteins; hyperactive antifreeze proteins
资金
- National Science Foundation (NSF)
- Marie Curie reintegration grant
- Israel Science Foundation (ISF)
- European research council (ERC)
- Canadian Institute of Health Research (CIHR)
- Lady Davis Fellowship Trust
- Wenner-Gren Foundation
- John Simon Guggenheim Foundation
- Swedish Research Council
Antifreeze proteins (AFPs) evolved in many organisms, allowing them to survive in cold climates by controlling ice crystal growth. The specific interactions of AFPs with ice determine their potential applications in agriculture, food preservation and medicine. AFPs control the shapes of ice crystals in a manner characteristic of the particular AFP type. Moderately active AFPs cause the formation of elongated bipyramidal crystals, often with seemingly defined facets, while hyperactive AFPs produce more varied crystal shapes. These different morphologies are generally considered to be growth shapes. In a series of bright light and fluorescent microscopy observations of ice crystals in solutions containing different AFPs, we show that crystal shaping also occurs during melting. In particular, the characteristic ice shapes observed in solutions of most hyperactive AFPs are formed during melting. We relate these findings to the affinities of the hyperactive AFPs for the basal plane of ice. Our results demonstrate the relation between basal plane affinity and hyperactivity and show a clear difference in the ice-shaping mechanisms of most moderate and hyperactive AFPs. This study provides key aspects associated with the identification of hyperactive AFPs.
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