Point mutagenesis and cocrystallization of wild-type and mutant proteins: A study of solid-phase coexistence in two-dimensional protein arrays

被引：7

作者：

Farah, SJ ^{[1
]}

Wang, SW ^{[1
]}

Chang, WH ^{[1
]}

Robertson, CR ^{[1
]}

Gast, AP ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem Engn, Stanford, CA 94305 USA

来源：

LANGMUIR | 2001年 / 17卷 / 19期

关键词：

D O I：

10.1021/la010227n

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We are studying the molecular organization of protein arrays using two-dimensional streptavidin crystals bound to biotinylated lipid monolayers at the air-water interface. We constructed a mutant form of the streptavidin protein that successfully alters the molecular organization of the streptavidin crystals. Cocrystallization of streptavidin carrying this single targeted point mutation with wild-type streptavidin yields two-dimensional crystals displaying a chiral morphology with molecular coexistence, indicating a solid-phase transition. The phase coexistence and resulting morphologies are reminiscent of two-dimensional crystal behavior of wild-type streptavidin near its isoelectric point, and this analogy is discussed. These results demonstrate the potential to manipulate protein array formation through point mutagenesis and cocrystallization.

引用

页码：5731 / 5735

页数：5

共 19 条

[11] SOLVING THE STRUCTURE OF HUMAN H-FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS [J].