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Updated: Jun 18, 2026

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
Published on: February 4, 2013
An ice-binding protein from an Arctic population of American dunegrass, Leymus mollis
Todd L Sformo1,2, James A Raymond3
1Department of Wildlife Management, North Slope Borough, Utqiaġvik, Alaska, 99723, USA.
Abstract:
Several cold-hardy grasses have been shown to have ice-binding proteins (IBPs) that protect against freeze-thaw injury. Here, we looked for IBP activity in an Alaskan coastal grass, Leymus mollis (Pooidae), that had not previously been examined. Rhizome tissue had strong ice-structuring and ice recrystallization inhibiting (IRI) activities, indicating the probable presence of IBPs. The gene sequence of an IBP was obtained. The sequence encoded a 118-amino acid IRI domain composed of eight repeats and that was 80% identical to the IRI domain of the IBP of perennial ryegrass Lolium perenne. The predicted 3D structure of the IRI domain had eight beta-roll coils like those in L. perenne IBP.
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