ATP-induced structural change of the thermosome is temperature-dependent (2001)
Gutsche, I., Holzinger, J., Rauh, N., Baumeister, W., May, R. P.
Protein folding by chaperonins is powered by ATP binding and hydrolysis. ATPase activity drives the folding machine through a series of conformational rearrangements, extensively described for the...
Conformational rearrangements of an archaeal chaperonin upon ATPase cycling (2000)
Gutsche, I., Holzinger, J., Rößle, M., Heumann, H., Baumeister, W., May, R. P.
Chaperonins are double-ring protein assemblies with a central cavity that provides a sequestered environment for in vivo protein folding. Their reaction cycle is thought to consist of a...
Kruif De, C.G., Rouw, P.W., Briels, W.J., Duits, M.H.G., Vrij, A., May, R.P.
Small-angle neutron-scattering structure factor measurements were made on sterically stabilized silica spheres dispersed in benzene up to volume fractions of 0.30. Benzene is only a marginal solvent...