chaperonins & substrate proteins

last update:
01.10.2001

Studies of the conformation of substrate proteins bound to the chaperonin GroEL

Post-doctoral research at the Oxford Centre for Molecular Sciences (OCMS) 1993-- 1996, with Dr Sheena E. Radford, funded by long-term fellowships from EMBO (first year) and FEBS (another two years). The project, which was a collaboration with the group of F.U. Hartl (New York) focussed on the structure and dynamics of the chaperonins GroEL and GroES and their bound substrates. Methods included hydrogen exchange labelling as monitored by NMR and electrospray ionization mass spectrometry, spectroscopy (CD, fluorescence, etc.) stopped flow methods (CD, fluorescence) and standard biochemical techniques. Fig: Crystallographic structure of a GroEL-substrate complex (not from this work).

Post-doctoral research at the Oxford Centre for Molecular Sciences (OCMS) 1993-- 1996, with Dr Sheena E. Radford, funded by long-term fellowships from EMBO (first year) and FEBS (another two years). The project, which was a collaboration with the group of F.U. Hartl (New York) focussed on the structure and dynamics of the chaperonins GroEL and GroES and their bound substrates. Methods included hydrogen exchange labelling as monitored by NMR and electrospray ionization mass spectrometry, spectroscopy (CD, fluorescence, etc.) stopped flow methods (CD, fluorescence) and standard biochemical techniques.

Fig: Crystallographic structure
of a GroEL-substrate complex
(not from this work).

Publications:

Robinson CV, Groß M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM & Radford SE (1994): Nature 372, 646-651 -- Conformation of GroEL-bound alpha- lactalbumin probed by mass spectrometry
Robinson CV, Groß M, Miranker A, Radford SE, Aplin RT & Dobson CM (1995) in: Perspectives on Protein Engineering (M. Geisow and N.N., eds), Mayflower ..., pp 57- 59 -- Protein structure and folding by mass spectrometry
Groß M, Robinson CV, Mayhew M, Hartl FU, Radford, SE (1996): Protein Science 5, 2506-2513
Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
Chung E, Nettleton E, Morgan C, Groß M, Miranker, A, Dobson CM, Radford SE, Robinson CV (1997) Protein Science 6, 1316-1324
Coyle J, Jaeger J, Groß M, Robinson CV, Radford SE (1997) Folding & Design 2, R93-R104
Structural and mechanistic consequences of polypeptide binding by GroEL
Robinson CV, Groß M, Radford SE (1997) Methods in Enzymology 290, 296-313
Probing the conformation of GroEL-bound substrate proteins by mass spectrometry

External links to:

the chaperonin home page
the Molecular Chaperone Club (UK)

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Dr Michael Groß

michael@michaelgross.co.uk

www.michaelgross.co.uk

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