CARS and Raman spectroscopy of function-related conformational changes of chymotrypsin

We report on the comparative analysis of the conformation‐sensitive bands of free enzyme (chymotrypsin), liganded enzyme (chymotrypsin anthranilate) and enzyme complex with 18‐crown‐6. The studies were carried out by Raman scattering spectroscopy and polarization‐sensitive coherent anti‐Stokes Raman scattering spectroscopy (CARS). The bands of tyrosine and tryptophan residues, disulfide bridges and amide I and amide III were analyzed. It is concluded that the conformation of the enzyme changes much more in the case of liganding than in the case of the formation of a complex with the crown ether. Copyright © 2000 John Wiley & Sons, Ltd.