Abstract
Functional activity of protein molecules is closely related with their conformational changes. Binding site of the enzyme molecule adopts itself to the ligand by changing the torsion angles, H-bonds, relative displacements of the corresponding amino-acid residues. All these changes may be easily traced by methods of vibrational spectroscopy and its application to the study of the enzyme-substrate interaction in the recent years was really fruitful [1]. In contrast to the conventional approach when the methods of resonance Raman spectroscopy are used for the study of the chromophores inside protein molecule this work is aimed at investigation of the conformational changes of the protein molecule as a whole induced by its interaction with ligands.
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