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Polarization‐Sensitive CARS of the Amide I Band of Pure and Liganded Chymotrypsin
Author(s) -
Chikishev A. Yu.,
Koroteev N. I.,
Otto C.,
Greve J.
Publication year - 1996
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/(sici)1097-4555(199612)27:12<893::aid-jrs48>3.0.co;2-y
Subject(s) - chemistry , chymotrypsin , raman spectroscopy , analyser , amide , polarization (electrochemistry) , peptide bond , peptide , crystallography , substrate (aquarium) , analytical chemistry (journal) , trypsin , enzyme , chromatography , biochemistry , optics , physics , oceanography , geology
Polarization‐sensitive coherent anti‐Stokes Raman scattering (PSCARS) is used to investigate the secondary structure of the protein chymotrypsin, both free and bound to antranilic acid. Advantage is taken of the extreme sensitivity of the PSCARS spectra to the orientation of the analyser. Clear changes are observed in the protein spectra as a result of binding to antranilic acid. It is concluded that PSCARS can be fruitfully applied to detect changes in the bonds of the peptide backbone of enzymatic proteins as a result of substrate binding.