A Diminished Role for Hydrogen Bonds in Antifreeze Protein Binding to Ice
详细信息    查看全文
文摘
The most abundant isoform (HPLC-6) of type I antifreeze protein(AFP1) in winter flounderis a 37-amino-acid-long, alanine-rich, -helical peptide, containingfour Thr spaced 11 amino acids apart.It is generally assumed that HPLC-6 binds ice through ahydrogen-bonding match between the Thr andneighboring Asx residues to oxygens atoms on the {201} planeof the ice lattice. The result is a loweringof the nonequilibrium freezing point below the melting point (thermalhysteresis). HPLC-6, and twovariants in which the central two Thr were replaced with either Ser orVal, were synthesized. The Servariant was virtually inactive, while only a minor loss of activity wasobserved in the Val variant. CD,ultracentrifugation, and NMR studies indicated no significantstructural changes or aggregation of thevariants compared to HPLC-6. These results call into question therole of hydrogen bonds and suggesta much more significant role for entropic effects and van der Waalsinteractions in binding AFP to ice.

© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号

地址:北京市海淀区学院路29号 邮编:100083

电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700