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Protein Crystallisation on Chemically Modified Mica Surfaces by Giuseppe Falini; Simona Fermani; Giovanna Conforti; Alberto Ripamonti is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Protein Crystallisation on Chemically Modified Mica Surfaces about?

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.

Who reads Protein Crystallisation on Chemically Modified Mica Surfaces?

Author

Giuseppe Falini; Simona Fermani; Giovanna Conforti; Alberto Ripamonti

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)