Nmr spectroscopy to study the factors controlling the folding/unfolding process in paramagnetic metalloproteins
FP4 — Training and Mobility of Researchers
- Duration
- 1997-12-01 → 1999-12-31
- EU contribution
- —
- Participants
- 2
- Scheme
- RGI
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Project objective
The objective of the project is the use of multinuclear (1H, 13C, 15N) NMR spectroscopy to study the folding/unfolding process of paramagnetic metalloproteins such as c (horse heart, yeast) and b type (b5 from rat) cytochromes, their mutants and the isotopically enriched cyt b5 (rat). NMR spectroscopic techniques will be applied to partially unfolded states of the above proteins in order to probe: (i) the protein sites where the unfolding process starts; (ii) the dependence of the unfolding process on the redox state of the iron; (iii) the changes induced to the heme prosthetic group and their dependence on the presence (cyt c), or not (cyt b), of covalent links with the protein frame. The dynamical properties of the partially unfolded proteins will be studied by analyzing the exchange rates of amide protons and by performing MD calculations. The acquisition of J-correlated spectra using 500, 600, and 800 MHz magnetic fields will provide valuable information of the average structure of intermediate protein species exploiting the magnetic field dependence of nuclear resolution. The solution structures will be refined by using unconventional paramagnetic constraints for the paramagnetic systems. These constraints which are based on nuclear relaxation and hyperfine shifts (pseudocontact shifts) are long range iron nucleus constraints and are particularly useful in partially unfolded proteins. . . . .
Original text from CORDIS.
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Data: CORDIS, © European Union