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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.

SUBMITTER: Fafarman AT 

PROVIDER: S-EPMC2516909 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

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Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins.

Fafarman Aaron T AT   Webb Lauren J LJ   Chuang Jessica I JI   Boxer Steven G SG  

Journal of the American Chemical Society 20061001 41


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 t  ...[more]

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