| Full text | |
| Author(s): |
Total Authors: 2
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| Affiliation: | [1] Univ Calif Berkeley, Dept Chem & Biomol Engn, Berkeley, CA 94720 - USA
[2] Univ Sao Paulo, Dept Chem Engn, Sao Paulo, SP - Brazil
Total Affiliations: 2
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| Document type: | Journal article |
| Source: | International Journal of Biological Macromolecules; v. 78, p. 257-265, JUL 2015. |
| Web of Science Citations: | 0 |
| Abstract | |
Toward the development of an electrostatic model for enzyme catalysis, the active site of the enzyme is represented by a cavity whose surface (and beyond) is populated by electric charges as determined by pH and the enzyme's structure. The electric field in the cavity is obtained from electrostatics and a suitable computer program. The key chemical bond in the substrate, at its ends, has partial charges with opposite signs determined from published force-field parameters. The electric field attracts one end of the bond and repels the other, causing bond tension. If that tension exceeds the attractive force between the atoms, the bond breaks; the enzyme is then a successful catalyst. To illustrate this very simple model, based on numerous assumptions, some results are presented for three hydrolases: hen-egg white lysozyme, bovine trypsin and bovine ribonuclease. Attention is given to the effect of pH. (C) 2015 Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 12/23860-2 - Study of the relationship between the biological activity of proteins and process conditions in bioproduct downstream operations |
| Grantee: | Pedro de Alcântara Pessôa Filho |
| Support Opportunities: | Scholarships abroad - Research |