Abstract
Ab initio quantum mechanicalmolecular mechanical method is combined with the polarized protein-specific charge to study the chemical reactions catalyzed by protein enzymes. Significant improvement in the accuracy and efficiency of free-energy simulation is demonstrated by calculating the free-energy profile of the primary proton transfer reaction in triosephosphate isomerase. Quantitative agreement with experimental results is achieved. Our simulation results indicate that electronic polarization makes important contribution to enzyme catalysis by lowering the energy barrier by as much as 3 kcalmol.
Original language | English (US) |
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Article number | 205101 |
Journal | Journal of Chemical Physics |
Volume | 134 |
Issue number | 20 |
DOIs | |
State | Published - May 28 2011 |
ASJC Scopus subject areas
- General Physics and Astronomy
- Physical and Theoretical Chemistry