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ATP and the Core "α-Crystallin" Domain of the Small Heat-shock Protein αB-crystallin
1999
Journal of Biological Chemistry
Electrospray ionization mass spectrometry (ESI-LC/ MS) of tryptic digests of human ␣B-crystallin in the presence and absence of ATP identified four residues located within the core "␣-crystallin" domain, Lys 82 , Lys 103 , Arg 116 , and Arg 123 , that were shielded from the action of trypsin in the presence of ATP. In control experiments, chymotrypsin was used in place of trypsin. The chymotryptic fragments of human ␣B-crystallin produced in the presence and absence of ATP were analyzed using
doi:10.1074/jbc.274.42.30190
pmid:10514509
fatcat:e7o4zll4w5bs5gcpnvekm2yusm