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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Protein crystallisation on chemically modified mica surfaces.
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Protein crystallisation on chemically modified mica surfaces.

机译:蛋白质结晶化学改性云母的表面。

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摘要

Chemically modified mica sheets have been tested as heterogeneous nucleant surfaces for lysozyme, concanavalin A and thaumatin. Smooth mica surfaces with reduced hydrophilic properties and different density of ionisable groups have been prepared by a silanisation reaction using mixtures of n-propyltriethoxysilane and 3-aminopropyltriethoxysilane in different percentages starting from 0 to 100% of aminosilane. The crystallisation experiments were carried out with the hanging drop vapour diffusion technique. The results suggest that these mica surfaces act as heterogeneous nucleant agents, whose effectiveness is due to non-specific attractive and local interactions between charged residues of the protein and the ionisable groups on the mica surfaces.
机译:化学改性云母片测试作为溶菌酶异构形成核的表面,伴刀豆球蛋白A和奇异果甜蛋白。表面亲水属性和减少不同密度的ionisable组由silanisation反应使用n-propyltriethoxysilane混合物,3-aminopropyltriethoxysilane在不同从0到100%的比例aminosilane。进行悬滴蒸汽扩散技术。这些云母表面作为异构形成核的剂,由于其有效性非特异性的吸引力和本地交互带电残基的蛋白质和之间ionisable组在云母表面。

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