@inbook{e45edd41060d4e46becc26425cd4fd71,
title = "Accurate Calculation of Electric Fields Inside Enzymes",
abstract = "The specific electric field generated by a protease at its active site is considered as an important source of the catalytic power. Accurate calculation of electric field at the active site of an enzyme has both fundamental and practical importance. Measuring site-specific changes of electric field at internal sites of proteins due to, eg, mutation, has been realized by using molecular probes with C[dbnd]O or C[tbnd]N groups in the context of vibrational Stark effect. However, theoretical prediction of change in electric field inside a protein based on a conventional force field, such as AMBER or OPLS, is often inadequate. For such calculation, quantum chemical approach or quantum-based polarizable or polarized force field is highly preferable. Compared with the result from conventional force field, significant improvement is found in predicting experimentally measured mutation-induced electric field change using quantum-based methods, indicating that quantum effect such as polarization plays an important role in accurate description of electric field inside proteins. In comparison, the best theoretical prediction comes from fully quantum mechanical calculation in which both polarization and inter-residue charge transfer effects are included for accurate prediction of electrostatics in proteins.",
keywords = "Charge transfer effect, Electric field, Molecular fragmentation, Polarization effect, Stark shift",
author = "X. Wang and X. He and Zhang, {J. Z.H.}",
note = "Funding Information: This work was supported by the National Natural Science Foundation of China (Grant nos. 21433004, 21303057, and 11547164) and Shanghai Putuo District (Grant no. 2014-A-02). X.H. is also supported by the Specialized Research Fund for the Doctoral Program of Higher Education (Grant no. 20130076120019) and the Fundamental Research Funds for the Central Universities. We thank the Supercomputer Center of East China Normal University for providing us computational time. Publisher Copyright: {\textcopyright} 2016 Elsevier Inc.",
year = "2016",
doi = "10.1016/bs.mie.2016.05.043",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "45--72",
booktitle = "Computational Approaches for Studying Enzyme Mechanism Part B",
address = "United States",
}