Open Access. Powered by Scholars. Published by Universities.®
Social and Behavioral Sciences Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Social and Behavioral Sciences
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
J. A. Aquilina
The small heat shock protein, α-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of particular importance in the human lens, where proteins are exposed to post-translational modifications over the life-time of an individual. Here, we examine the structural and functional consequences of one particular modification of αA-crystallin involving the truncation of 5 C-terminal residues (αA1–168). Using novel mass spectrometry approaches and established biophysical techniques, we show that αA1–168 forms oligomeric assemblies with a lower average molecular mass than wild-type αA-crystallin (αAWT). Also apparent from the mass spectra of both αAWT and αA1–168 …
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J Andrew Aquilina
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J Andrew Aquilina
J. A. Aquilina
The quaternary structure of alpha-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of alpha-crystallin. For total alpha-crystallin isolated directly from fetal calf lens using size-based chromatography, the alpha B-crystallin subunit was found to be preferentially dissociated from the oligomers, despite being significantly less abundant overall than the alpha A-crystallin subunits. Furthermore, upon mixing molar equivalents of purified alpha A- and alpha B-crystallin, the levels of their dissociation were found to decrease and increase, respectively, with time. Interestingly …