Folding of single-tryptophan mutants of hpr

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Project objective

At present a first description of the folding behaviour of HPr has been obtained by a combined use of DSC, CD, NMR and fluorescence enhancement upon ANS-binding. The unfolding is described adequately as a two-state process. Both equilibrium measurements (DSC, NMR, CD and W spectroscopy) and kinetic experiments (stopped flow spectroscopy, rapid-mixing NMR) have led to this conclusion. The folding of HPr is remarkably slow, in stopped-flow experiments no observable events take place within the instrumental dead-time. Our strategy is to replace the four phenylalanines positioned at different sites in the structure by tryptophans, to obtain a more detailed description of HPr's folding and which residues play a key role in the stability and folding. Comparison with the structural related AcP will give us insight in what way the final fold determines the folding pathway. Using this approach we fully employ the potential of using above techniques and contributions of the laboratories involved.

Original text from CORDIS.

Participants

• UNIVERSITY OF GRONINGEN · GRONINGENCoordinatorNetherlands
• Not availableCity levelNetherlands

Links

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