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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
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 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
Small Heat Shock Protein Activity Is Regulated By Variable Oligomeric Substructure, J. L. Benesch, M. Ayoub, C. V. Robinson, J. A. Aquilina
J. A. Aquilina
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 …
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 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 …
Tandem Mass Spectrometry Of Deprotonated Iodothyronines, A. M. Couldwell, M. C. Thomas, Todd Mitchell, A. Hulbert, Stephen J. Blanksby
Tandem Mass Spectrometry Of Deprotonated Iodothyronines, A. M. Couldwell, M. C. Thomas, Todd Mitchell, A. Hulbert, Stephen J. Blanksby
Stephen Blanksby
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 …
Statistical Contributions To Proteomic Research, Jeffrey S. Morris, Keith A. Baggerly, Howard B. Gutstein, Kevin R. Coombes
Statistical Contributions To Proteomic Research, Jeffrey S. Morris, Keith A. Baggerly, Howard B. Gutstein, Kevin R. Coombes
Jeffrey S. Morris
Proteomic profiling has the potential to impact the diagnosis, prognosis, and treatment of various diseases. A number of different proteomic technologies are available that allow us to look at many proteins at once, and all of them yield complex data that raise significant quantitative challenges. Inadequate attention to these quantitative issues can prevent these studies from achieving their desired goals, and can even lead to invalid results. In this chapter, we describe various ways the involvement of statisticians or other quantitative scientists in the study team can contribute to the success of proteomic research, and we outline some of the …