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Two-dimensional crystallization of streptavidin: in pursuit of the molecular origins of structure, morphology, and thermodynamics

机译:链霉亲和素的二维结晶:追求结构,形态和热力学的分子起源

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摘要

The streptavidin two-dimensional (2D) crystallization model has served as a paradigm for molecular self-assembly at interfaces. We have developed quantitative Brewster angle microscopy for the in situ measurement of spatially resolved relative protein: surface densities. This allows investigation of both the thermodynamics and morphologies of 2D crystal growth. For crystal structure analysis, we employ TEM on grown crystals transferred to solid substrates. Comparison of results between commercially available streptavidin, recombinant streptavidin, and site-directed streptavidin mutants has provided insight into the proteinprotein and protein-lipid interactions that underlie 2D crystallization.
机译:链霉亲和素二维(2D)结晶模型已成为界面分子自组装的范例。我们开发了定量布鲁斯特角显微镜,用于原位测量空间分辨的相对蛋白:表面密度。这允许研究2D晶体生长的热力学和形态。对于晶体结构分析,我们对转移到固体基质上的生长晶体采用TEM。对市售链霉亲和素,重组链霉亲和素和定点链霉亲和素突变体之间的结果进行比较,可以深入了解构成2D结晶的蛋白质和蛋白质-脂质相互作用。

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