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
Activity losses among T4 lysozyme variants after adsorption to colloidal silica
โ Scribed by C. K. Bower; Q. Xu; J. McGuire
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 104 KB
- Volume
- 58
- Category
- Article
- ISSN
- 0006-3592
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โฆ Synopsis
Maintaining a specific molecular conformation is essential for the proper functioning of an enzyme. A substantial loss of catalytic activity can occur from the displacement caused by even a single amino acid substitution. Activity may also be lost as an enzyme undergoes a conformational change during adsorption. In this study, we investigated the effect of thermostability on the activities of three T4 lysozyme variants after adsorption to 9 nm colloidal silica particles. Less-stable T4 lysozyme variants lost more activity after adsorption than did more stable variants, apparently because they experienced more extensive structural alteration.
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