| Autor: |
Baines C; School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom., Sargeant J; Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom., Fage CD; Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom., Pugh H; Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom., Alkhalaf LM; Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom., Challis GL; Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom.; Warwick Integrative Synthetic Biology Centre, University of Warwick, Coventry CV4 7AL, United Kingdom.; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria 3800, Australia.; ARC Centre of Excellence for Innovations in Peptide and Protein Science, Monash University, Clayton, Victoria 3800, Australia., Oldham NJ; School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom. |
| Abstrakt: |
Collision-induced unfolding (CIU) of protein ions, monitored by ion mobility-mass spectrometry, can be used to assess the stability of their compact gas-phase fold and hence provide structural information. The bacterial elongation factor EF-Tu, a key protein for mRNA translation in prokaryotes and hence a promising antibiotic target, has been studied by CIU. The major [M + 12H] 12+ ion of EF-Tu unfolded in collision with Ar atoms between 40 and 50 V, corresponding to an E lab energy of 480-500 eV. Binding of the cofactor analogue GDPNP and the antibiotic enacyloxin IIa stabilized the compact fold of EF-Tu, although dissociation of the latter from the complex diminished its stabilizing effect at higher collision energies. Molecular dynamics simulations of the [M + 12H] 12+ EF-Tu ion showed similar qualitative behavior to the experimental results. |
