부산대학교 도서관

Cathepsin-L, a protease known to proteolyse histone tails in cells, is introduced as a novel enzyme for HX-MS. Cathepsin-L generates overlapping N-terminal peptides, improving coverage of histone tails that are poorly represented in HX-MS employing pepsin alone. Cathepsin-L/pepsin is employed to investigate in-solution dynamics of H3 and H4 monomers. Rapid deuteration of the tails is indicative of unfolded polypeptides, whereas extensive bimodal distributions detected in the histone-folds reveal cooperative unfolding events.