The role of molecular crowding on protein structure, dynamics, and function is an emerging topic of biophysical chemistry. The molecular mechanism of crowding action on proteins has been probed extensively in recent years. These studies demonstrated that the effect of crowded intracellular environment of a cell can be mimicked by including variable-sized and types of crowding agents in protein assays. In the present study, the effects of a few common synthetic molecular crowders (monomers and polymers) have been investigated on the function of <i>Escherichia coli</i> prolyl-tRNA synthetase (Ec ProRS). Ec ProRS functions as a catalyst for the attachment of proline onto the cognate transfer ribonucleic acid and is vital for protein synthesis. A polymer cosolute could affect enzyme function mainly through excluded volume and hard interactions, while a monomer could employ soft, chemical interactions. These differences in mechanism have been explored by using intrinsic tryptophan fluorescence spectroscopy. Herein, results of our spectroscopic study will be presented.

Exploring the effects of monomer and polymer cosolutes on the conformation of <i>Escherichia coli</i> prolyl-tRNA synthetase using intrinsic tryptophan fluorescence spectroscopy

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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Exploring the effects of monomer and polymer cosolutes on the conformation of Escherichia coli prolyl-tRNA synthetase using intrinsic tryptophan fluorescence spectroscopy