Work

Site-Specific Conversion of Cysteine Thiols into Thiocyanate Creates an IR Probe for Electric Fields in Proteins

Year: 2006

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja0650403

Authors: Aaron T. Fafarman, Lauren J. Webb, Jessica I. Chuang, Steven G. Boxer

Institution: Stanford University

Language: English

Topic: Spectroscopy Techniques in Biomedical and Chemical Research

Subfield: Biophysics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Vibrational Stark Effect in Human Aldose Reductase, ELECTROSTATICS AND DYNAMICS IN MYOGLOBIN MUTANTS, G825520288