Activity losses among T4 lysozyme charge variants after adsorption to colloidal silica

Enzyme structure and function depend to some extent on enzyme net charge and charge location. Altering the charge of even a single residue may affect the interaction between enzyme and substrate such that all catalytic activity is lost. In this study we investigated the effect of net charge and char...

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Veröffentlicht in:	Biotechnology and bioengineering 1999-08, Vol.64 (3), p.373-376
Hauptverfasser:	Bower, C. K., Sananikone, S., Bothwell, M. K., McGuire, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adsorption Bacteriophage T4 - enzymology bacteriophage T4 lysozyme Bacteriophages Biological and medical sciences Biotechnology Catalyst activity charge-changed mutants Circular Dichroism Colloids Colloids - chemistry Electrostatics Enzyme engineering Fundamental and applied biological sciences. Psychology Methods. Procedures. Technologies Micrococcus - enzymology Miscellaneous Models, Molecular Molecular orientation Molecular structure Muramidase - chemistry Mutagenesis Mutagenesis, Site-Directed Phage T4 Silica silica nanoparticles Silicon Dioxide - chemistry synthetic enzyme variants
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