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The function of ScHSP26 is thermally controlled: the heat shock that causes the destabilization of target proteins leads to its activation as a molecular chaperone. We investigate the structural and dynamical properties of ScHSP26 oligomers through a combination of multiangle light scattering, fluorescence spectroscopy, NMR spectroscopy, and mass spectrometry. We show that ScHSP26 exists as a heterogeneous oligomeric ensemble at room temperature. At heat-shock temperatures, two shifts in equilibria are observed: toward dissociation and to larger oligomers. We examine the quaternary dynamics of these oligomers by investigating the rate of exchange of subunits between them and find that this not only increases with temperature but proceeds via two separate processes. This is consistent with a conformational change of the oligomers at ele...
This report was produced by Jane Harford and Xiangqun Ju.
Martina Weber, Sandro Lambeck, Nadine Ding, Stefanie Henken, Matthias Kohl, Hans P. Deigner, David P. Enot, Emeka I. Igwe, Lucien Frappart, Michael Kiehntopf, Ralf A. Claus, Thomas Kamradt, Debra Weih, Yoram Vodovotz, David E. Briles, Abiodun D. Ogunniyi, James C. Paton, Ulrich A. Maus and Michael Bauer
Gavin D. Richardson, Hisham Bazzi, Katherine A. Fantauzzo, James M. Waters, Heather Crawford, Phil Hynd, Angela M. Christiano and Colin A. B. Jahoda
R H Wallace, S F Berkovic, R A Howell, G R Sutherland, J C Mulley
©2005 COPYRIGHT SPIE--The International Society for Optical Engineering. Downloading of the abstract is permitted for personal use only.
© 1995 Australian Society of Anaesthetists
Souleiman Hasan, Kalpa Gunaratna, Yongrui Qin, Edward Curry
Hoffmann, D. ; Moore, J. ; Roder, D.
