Site-directed oxidative protein crosslinking

Many important biological processes are catalyzed by large multiprotein complexes. A central goal in the study of these ''protein machines'' is to characterize the organization of proteins and to determine if this organization changes during the catalytic cycle. For this purpose, methodology has been developed to deliver a latent crosslinking reagent to a particular protein in complex solutions. When activated, the crosslinking of the tagged protein to its nearest neighbors occurs without large-scale covalent modifications elsewhere in the complex. Recent technical advances in this methodology are described (C) 1997 Elsevier Science Ltd.