期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 410, 期 2, 页码 238-245出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/S0003-9861(02)00697-5
关键词
antifreeze protein; antifreeze peptide; FTIR; rye grass; Lolium perenne; ice recrystallization; ice binding; ice crystal plane
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 (10 (1) over bar0) 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. (C) 2002 Elsevier Science (USA). All rights reserved.
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