Social and Behavioral Sciences Commons^™

R120g Αb-Crystallin Promotes The Unfolding Of Reduced Α-Lactalbumin And Is Inherently Unstable., T. M. Treweek, A. Rekas, R. A. Lindner, Mark J. Walker, J. A. Aquilina, C. V. Robinson, J. Horwitz, M. Der Perng, R. A. Quinlan, J. A. Carver

J. A. Aquilina

α-Crystallin is the principal lens protein which, in addition to its structural role, also acts as a molecular chaperone, to prevent aggregation and precipitation of other lens proteins. One of its two subunits, αB-crystallin, is also expressed in many non-lenticular tissues, and a natural missense mutation, R120G, has been associated with cataract and desminrelated myopathy, a disorder of skeletal muscles (Vicart et al., 1998, Nature Genet. 20:92-95). In the present study, real-time 1H NMR spectroscopy showed that the ability of R120G αB-crystallin to stabilize the partially folded, molten globule state of α- lactalbumin was significantly reduced in comparison with wild …