SITE-DIRECTED OXIDATIVE PROTEIN CROSS-LINKING

Many important biological processes are catalyzed by large multiprotei n complexes. A central goal in the study of these ''protein machines'' is to characterize the organization of proteins and to determine if t his organization changes during the catalytic cycle. For this purpose, methodology has been developed to deliver a latent crosslinking reage nt to a particular protein in complex solutions. When activated, the c rosslinking of the tagged protein to its nearest neighbors occurs with out large-scale covalent modifications elsewhere in the complex. Recen t technical advances in this methodology are described (C) 1997 Elsevi er Science Ltd.