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化学学报
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化学学报 ›› 2007, Vol. 65 ›› Issue (17): 1767-1772. 上一篇    下一篇

研究论文

分子间相互作用对蛋白质晶体生长的影响

戴国亮*, 彭玲, 解莹, 康琦, 胡文瑞   

  1. (中国科学院力学研究所国家微重力实验室 北京 100080)
  • 投稿日期:2006-11-20 修回日期:2007-03-19 发布日期:2007-09-14
  • 通讯作者: 戴国亮

Effect of Intermolecular Interaction on Protein Crystal Growth

DAI Guo-Liang*; PENG Ling; XIE Ying; KANG Qi; HU Wen-Rui   

  1. (National Microgravity Laboratory, Institute of Mechanics, Chinese Academy of Sciences, Beijing 100080)
  • Received:2006-11-20 Revised:2007-03-19 Published:2007-09-14
  • Contact: DAI Guo-Liang

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1080

被引次数

15 | 1

采用原子力显微镜对溶菌酶和刀豆蛋白A的分子间相互作用力的情况进行了研究, 并用动态光散射研究了此二种分子间相互作用力有较大差异的蛋白质在晶体生长条件和非生长条件下, 溶液中的聚集体的状态(大小和分散度)随浓度和温度的变化情况. 实验结果表明, 范德华力强的刀豆蛋白A在成核前, 溶液中的聚集体不能很快转变为生长基元, 导致晶体生长时间长; 而范德华力弱的溶菌酶, 溶液中的聚集体可以很快转变成生长基元, 晶体生长时间也较短.

关键词: 分子间相互作用, 刀豆蛋白A, 溶菌酶, 聚集体, 晶体生长

The intermolecular interaction of lysozyme and concanavalin A were investigated by atomic force microscopy, respectively. The mean size and polydispersity of both lysozyme and concanavalin A aggregates in solution under crystallization and non-crystallization conditions as the function of protein concentration and temperature were studied by dynamic light scattering method. The results showed that the intermolecular interaction of protein molecules had a strong effect on nucleation during protein crystal growth. Because the van der Waals force among concanavalin A molecules was stronger than that among lysozyme molecules, the growth unit of concanavalin A crystal could not appear quickly after the precipita-tor was mixed with concanavalin A solution, which caused the longer crystal growth time than that for ly-sozyme.

Key words: intermolecular interaction, concanavalin A, lysozyme, aggregate, crystal growth