On the pH-optimum of activity and stability of proteins
β Scribed by Kemper Talley; Emil Alexov
- Book ID
- 105358096
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 265 KB
- Volume
- 78
- Category
- Article
- ISSN
- 0887-3585
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β¦ Synopsis
Abstract
Biological macromolecules evolved to perform their function in specific cellular environment (subcellular compartments or tissues); therefore, they should be adapted to the biophysical characteristics of the corresponding environment, one of them being the characteristic pH. Many macromolecular properties are pH dependent, such as activity and stability. However, only activity is biologically important, while stability may not be crucial for the corresponding reaction. Here, we show that the pHβoptimum of activity (the pH of maximal activity) is correlated with the pHβoptimum of stability (the pH of maximal stability) on a set of 310 proteins with available experimental data. We speculate that such a correlation is needed to allow the corresponding macromolecules to tolerate small pH fluctuations that are inevitable with cellular function. Our findings rationalize the efforts of correlating the pH of maximal stability and the characteristic pH of subcellular compartments, as only pH of activity is subject of evolutionary pressure. In addition, our analysis confirmed the previous observation that pHβoptimum of activity and stability are not correlated with the isoelectric point, pI, or with the optimal temperature. Proteins 2010. Β© 2010 WileyβLiss, Inc.
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