Structural characterization of a partly folded apomyoglobin intermediate

摘要: To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize native state. Proteins in partly folded states can be used dissect protein organizational hierarchies. A apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them two-dimensional 1H-NMR (nuclear magnetic resonance). Protons A, G, H helix regions are protected from exchange, while B E exchange freely. On basis these results structure myoglobin, a structural model presented for which compact subdomain retains remainder essentially unfolded.