01875nas a2200193   4500008004100000022001400041245009900055210006900154260007100223300001400294490000600308520115000314100001801464700002401482700001601506700001801522700001801540856012301558       2016                        eng d  a1948-718500aPick and choose the spectroscopic method to calibrate the local electric field inside proteins0 aPick and choose the spectroscopic method to calibrate the local   a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcJUL  a2456-24600 v73 a<p>Electrostatic interactions in proteins play a crucial role in determining the structure function relation in biomolecules. In recent years, fluorescent probes have been extensively employed to interrogate the polarity in biological cavities through dielectric constants or semiempirical polarity scales. A choice of multiple spectroscopic methods, not limited by fluorophores, along with a molecular level description of electrostatics involving solute-solvent interactions, would allow more flexibility to pick and choose the experimental technique to determine the local electrostatics within protein interiors. In this work we report that ultraviolet/visible-absorption, infrared-absorption, or C-13 NMR can be used to calibrate the local electric field in both hydrogen bonded and non-hydrogen bonded protein environments. The local electric field at the binding site of a serum protein has been determined using the absorption wavelength as well as the carbonyl stretching frequency of its natural steroid substrate, testosterone. Excellent agreement is observed in the results obtained from two independent spectroscopic techniques.</p>1 aHaldar, Tapas1 aKashid, Somnath, M.1 aDeb, Pranab1 aKesh, Sandeep1 aBagchi, Sayan  uhttps://library.ncl.res.in/content/pick-and-choose-spectroscopic-method-calibrate-local-electric-field-inside-proteins