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Fafarman, Aaron T.
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Publications (3/3 displayed)
- 2016High Chloride Doping Levels Stabilize the Perovskite Phase of Cesium Lead Iodidecitations
- 2013Chemically tailored dielectric-to-metal transition for the design of metamaterials from nanoimprinted colloidal nanocrystalscitations
- 2006Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteinscitations
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article
Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins
Abstract
The nitrile stretching mode of the thiocyanate moiety is a nearly ideal probe for measuring the local electric field arising from the organized environment of the interior of a protein. Nitriles were introduced into three proteins: ribonuclease S (RNase S), human aldose reductase (hALR2), and the reaction center (RC) of Rhodobacter capsulatus, through a facile synthetic scheme for the transformation of cysteine residues into thiocyanatoalanine. Vibrational Stark effect spectroscopy and Fourier transform infrared spectroscopy on the modified proteins demonstrated that thiocyanate residues are a highly general tool for probing electrostatic fields in proteins.