Monitoring of Human Haptoglobin-Hemoglobin Interaction Interface using H/D exchange and Chemical Cross-linking

摘要

More than 30 cross-links around all domains of human haptoglobin and 9 cross-links of haptoglobin-hemoglobin complex were identified (Fig. 3). New homology models of human haptoglobin and haptoglobin-hemoglobin complex based on acquired distance constraints were generated (Fig. 3). Hydrogen/deuterium exchange experiments showing that glycosylation of haptoglobin does not have any effect on solvent accesibility to protein and also revealing interaction site of haptoglobin-hemoglobin complex that is in really good agreement with novel homology model (Fig. 4). Molecular dynamics simulation which describe behavior of fully glycosylated haptoglobin-hamoglobin complex in solution was performed.