The physico-chemical characterization of a boiling stable antifreeze protein from a perennial grass (Lolium perenne)
| Autor: | Peter J. Lillford, Paul D. A. Pudney, Sarah Twigg, David I. Roper, M.-P Sevilla, A.J McArthur, Chris Holt, Chris Sidebottom, Sarah L. Buckley, J. H. Telford |
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| Rok vydání: | 2003 |
| Předmět: |
Hot Temperature
Biophysics Biochemistry Lolium perenne Protein Structure Secondary Protein structure Antifreeze protein Boiling Antifreeze Proteins Botany Spectroscopy Fourier Transform Infrared Escherichia coli Lolium Peptide bond Animals Binding site Molecular Biology Protein secondary structure Binding Sites biology Ice Fishes Temperature biology.organism_classification Protein Structure Tertiary Ice binding Electrophoresis Polyacrylamide Gel Peptides |
| Zdroj: | Archives of biochemistry and biophysics. 410(2) |
| ISSN: | 0003-9861 |
| Popis: | We have characterized a cold-induced, boiling stable antifreeze protein. This highly active ice recrystallization inhibition protein shows a much lower thermal hysteresis effect and displays binding behavior that is uncharacteristic of any AFP from fish or insects. Ice-binding studies show it binds to the (1 0 1 0) plane of ice and FTIR studies reveal that it has an unusual type of highly beta-sheeted secondary structure. Ice-binding studies of both glycosylated and nonglycosylated expressed forms indicate that it adsorbs to ice through the protein backbone. These results are discussed in light of the currently proposed mechanisms of AFP action. |
| Databáze: | OpenAIRE |
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