Quantification of the electric field inside protein active sites and fullerenes.

While electrostatic interactions are exceedingly accountable for biological functions, no simple method exists to directly estimate or measure the electrostatic field in protein active sites. The electrostatic field inside the protein is generally inferred from the shift in the vibrational stretching frequencies of nitrile and thionitrile probes at the active sites through several painstaking and time-consuming experiments like vibrational Stark effect spectroscopy (VSS). Here we present a simple, fast, and reliable methodology, which can efficiently predict the vibrational Stark tuning rates (VSRs) of a large variety of probes within 10% error of the reported experimental data. Our methodology is based on geometry optimization and frequency calculations in the presence of an external electric field to predict the accurate VSR of newly designed nitrile/thionitrile probes. A priori information of VSRs is useful for difficult experiments such as catalytic/enzymatic study and in structural biology. We also applied our methodology successfully to estimate the electric field inside fullerenes and nano-onions, which is encouraging for researchers to adopt it for further applications in materials science and supramolecular chemistry.