Abstract
The main chemical approaches to the study of macromolecular structure and dynamics and to the elucidation of interbiopolymer contact points are considered and illustrated by particular examples. Primary attention is paid to the chemical footprinting and affinity modification methods. The use of bifunctional reagents for the study of nucleoprotein structure architecture is described. The ways of enhancing the selectivity of affinity modification available from the literature are analyzed with an emphasis on catalytically competent (superselective) labeling. The identification of proteins responsible for replication of the tickborne encephalitis virus by this method is described to demonstrate the possibility of the application of the method to multicomponent systems such as the nucleus fraction of infected cells.
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