Open Access. Powered by Scholars. Published by Universities.®

Physical Sciences and Mathematics Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 4 of 4

Full-Text Articles in Physical Sciences and Mathematics

Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J. Andrew Aquilina Jan 2010

Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J. Andrew Aquilina

Faculty of Science - Papers (Archive)

The quaternary structure of α-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 α-crystallin. For total α-crystallin isolated directly from fetal calf lens using size-based chromatography, the αB-crystallin subunit was found to be preferentially dissociated from the oligomers, despite being significantly less abundant overall than the αA-crystallin subunits. Furthermore, upon mixing molar equivalents of purified αA- and αB-crystallin, the levels of their dissociation were found to decrease and increase, respectively, with time. Interestingly though, dissociation of subunits …


Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina Aug 2008

Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina

Faculty of Science - Papers (Archive)

The alpha-crystallins are members of the small heat shock protein (sHSP) family of molecular chaperones which have evolved to minimize intracellular protein aggregation, however they are also implicated in a number of protein deposition diseases. In this study we have employed novel mass spectrometry techniques to investigate the changes in quaternary structure associated with this switch from chaperone to adjuvant of aggregation. We have replicated the oligomeric rearrangements observed for in vivo disease-related modifications, without altering the protein sequence, by refolding the alpha-crystallins in vitro. This refolding results in a loss of dimeric substructure concomitant with an augmentation of substrate …


Elucidation Of Double Bond Position In Unsaturated Lipids By Ozone Electrospray Ionization Mass Spectrometry (Ozesi-Ms), M. C. Thomas, Todd Mitchell, J. M. Deeley, D. G. Harman, R. C. Murphy, Stephen J. Blanksby Jun 2007

Elucidation Of Double Bond Position In Unsaturated Lipids By Ozone Electrospray Ionization Mass Spectrometry (Ozesi-Ms), M. C. Thomas, Todd Mitchell, J. M. Deeley, D. G. Harman, R. C. Murphy, Stephen J. Blanksby

Faculty of Science - Papers (Archive)

The position(s) of carbon-carbon double bonds within lipids can dramatically affect their structure and reactivity and thus has a direct bearing on biological function. Commonly employed mass spectrometric approaches to the characterization of complex lipids however, fail to localize sites of unsaturation within the molecular structure and thus cannot distinguish naturally occurring regioisomers. In a recent communication [Thomas, Mitchell, Blanksby in the Journal of the American Chemical Society, 2006, 128, 58-59] we have presented a new technique for the elucidation of double bond position in glycerophospholipids using ozone-induced fragmentation within the source of a conventional electrospray ionization mass spectrometer. Here …


Tandem Mass Spectrometry Of Deprotonated Iodothyronines, A. M. Couldwell, M. C. Thomas, Todd Mitchell, A. Hulbert, Stephen J. Blanksby Jun 2005

Tandem Mass Spectrometry Of Deprotonated Iodothyronines, A. M. Couldwell, M. C. Thomas, Todd Mitchell, A. Hulbert, Stephen J. Blanksby

Faculty of Science - Papers (Archive)

In order to assist with the development of more selective and sensitive methods for thyroid hormone analysis the [M-H]– anions of the iodothyronines; T4, T3, rT3, (3,5)-T2 and the non-iodinated thyronine (T0) have been generated by negative ion electrospray mass spectrometry. Tandem mass spectra of these ions were recorded on a triple quadrupole mass spectrometer and show a strong analogy with the fragmentation pathways of the parent compound, tyrosine. All iodothyronines also show significant abundances of the iodide anion in their tandem mass spectra, which represents an attractive target for MRM analysis, given that iodothyronines are the only iodine bearing …