Devries A L, Lin Y
Biochim Biophys Acta. 1977 Dec 20;495(2):388-92. doi: 10.1016/0005-2795(77)90395-6.
Sequence studies of an alpha-helical peptide antifreeze isolated from winter flounder have revealed the presence of clusters of polar amino acids separated by long sequences of alanine. Most of the polar residues are threonine and aspartate and are separated by 4.5 A, a repeat distance that also separates the oxygens in the ice lattice along the a-axis of an ice crystal. Such a lattice match suggests that the peptide binds to ice by means of hydrogen binding.
对从冬鲽中分离出的一种α-螺旋肽抗冻剂的序列研究表明，存在由长链丙氨酸序列隔开的极性氨基酸簇。大多数极性残基是苏氨酸和天冬氨酸，它们之间相隔4.5埃，这一重复距离也沿着冰晶的a轴将冰晶格中的氧隔开。这种晶格匹配表明该肽通过氢键结合到冰上。
