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PEDS Advance Access originally published online on January 31, 2008
Protein Engineering Design and Selection 2008 21(3):207-214; doi:10.1093/protein/gzm091
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain

Per Jemth1,2, Christopher M. Johnson1, Stefano Gianni1,3 and Alan R. Fersht1,4

1MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK

4 To whom correspondence should be addressed. E-mail: arf25{at}mrc-lmb.cam.ac.uk

The role of intermediates in the folding reaction of single-domain proteins is a controversial issue. It was previously shown by different methods that an on-pathway intermediate is populated in the presence of sodium sulphate during the folding of the FF domain from HYPA/FBP11. Here we demonstrate using analysis of the amplitudes of kinetic traces that this burst-phase folding intermediate is present at different salt concentration and at various pH, and is also found in roughly 30 site-directed mutants. The intermediate appears robust to changing conditions and thus fulfils an important criterion for a productive molecular species on the folding reaction pathway.

Keywords: FF domain/stopped-flow spectrometry/burst-phase analysis/kinetics/protein folding

Received December 14, 2007; revised December 14, 2007; accepted December 14, 2007.

2 Present address: Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, Uppsala SE-75123, Sweden

3 Present address: Dipartimento di Scienze Biochimiche ‘A. Rossi Fanelli’ and Istituto di Biologia e Patologia Molecolari del CNR, Università di Roma ‘La Sapienza’, Piazzale A. Moro 5, Rome 00185, Italy


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