Carver J A, Aquilina J A, Truscott R J, Ralston G B
Australian Cataract Research Foundation, University of Wollongong, NSW.
FEBS Lett. 1992 Oct 19;311(2):143-9. doi: 10.1016/0014-5793(92)81386-z.
Two-dimensional 1H NMR spectroscopy of bovine eye lens alpha-crystallin and its isolated alpha A and alpha B subunits reveals that these aggregates have short and very flexible C-terminal extensions of eight (alpha A) and ten (alpha B) amino acids which adopt little preferred conformation in solution. Total alpha-crystallin forms a tighter aggregate than the isolated alpha A and alpha B subunit aggregates. Our results are consistent with a micelle model for alpha-crystallin quaternary structure. The presence of terminal extensions is a general feature of those crystallins, alpha and beta, which form aggregates.
对牛眼晶状体α-晶体蛋白及其分离出的αA和αB亚基进行二维¹H核磁共振光谱分析，结果显示这些聚集体具有由八个（αA）和十个（αB）氨基酸组成的短且非常灵活的C末端延伸，它们在溶液中几乎没有偏好的构象。总的α-晶体蛋白形成的聚集体比分离出的αA和αB亚基聚集体更紧密。我们的结果与α-晶体蛋白四级结构的胶束模型一致。末端延伸的存在是那些形成聚集体的α和β晶体蛋白的一个普遍特征。
