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Full-Text Articles in Social and Behavioral Sciences
From Powder To Solution: Hydration Dependence Of Human Hemoglobin Dynamics Correlated To Body Temperature, A. M. Stadler, I. Digel, J. P. Embs, T. Unruh, Moeava Tehei, G. Zaccai, G. Büldt, G. M. Artmann
From Powder To Solution: Hydration Dependence Of Human Hemoglobin Dynamics Correlated To Body Temperature, A. M. Stadler, I. Digel, J. P. Embs, T. Unruh, Moeava Tehei, G. Zaccai, G. Büldt, G. M. Artmann
Faculty of Science - Papers (Archive)
A transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. In order to focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data revealed that …
The Small Heat-Shock Proteins Hspb2 And Hspb3 Form Well-Defined Heterooligomers In A Unique 3 To 1 Subunit Ratio, J. Den Engelsman, S. Baros, P. Y. W. Dankers, B. Kamps, W. T. Vree Egberts, C. S. Bode, L. A. Lane, J. A. Aquilina, J. L. P. Benesch, C. V. Robinson, W. W. De Jong, W. C. Boelens
The Small Heat-Shock Proteins Hspb2 And Hspb3 Form Well-Defined Heterooligomers In A Unique 3 To 1 Subunit Ratio, J. Den Engelsman, S. Baros, P. Y. W. Dankers, B. Kamps, W. T. Vree Egberts, C. S. Bode, L. A. Lane, J. A. Aquilina, J. L. P. Benesch, C. V. Robinson, W. W. De Jong, W. C. Boelens
Faculty of Science - Papers (Archive)
Various mammalian small heat-shock proteins (sHSPs) can interact with one another to form large polydisperse assemblies. In muscle cells, HSPB2/MKBP (myotonic dystrophy protein kinase-binding protein) and HSPB3 have been shown to form an independent complex. To date, the biochemical properties of this complex have not been thoroughly characterized. In this study, we show that recombinant HSPB2 and HSPB3 can be successfully purified from E.coli cells co-expressing both proteins. Nanoelectrospray ionization mass spectrometry and sedimentation velocity analytical ultracentrifugation analysis showed that HSPB2/B3 forms a series of well defined hetero-oligomers, consisting of 4, 8, 12, 16, 20 and 24 subunits, each maintaining …