|Affiliation:||Department of Physics and Chemistry
University of Palermo
Via Archirafi 36
Tel: (+39) 091-238-91729
Current research focuses on elucidating the characteristic features of proteins energy landscape. Time-resolved optical spectroscopy and wide-angle X-ray scattering are used to probe the dynamics of functionally relevant conformational changes in proteins.
The relationship between protein motions and the dynamics of the surrounding solvent is investigated with different experimental techniques (magnetic resonance, differential scanning calorimetry, dielectric spectroscopy, etc.) over a wide range of experimental parameters such as temperature and/or viscosity.
- Dynamics of protein allosteric transitions studied by time-resolved wide-angle X-ray scattering (TR-WAXS).
- Development of the in cell TR-WAXS technique: monitoring protein dynamics in a cellular environment.
- Native human neuroserpin and its pathological mutants: molecular basis of function and dysfunction.
- Allosteric effects on the polymerization of wild type and mutant serpins.
- TR-WAXS investigations of protein folding/unfolding induced by photoactivated pH jumps.
- Spectroscopic investigation of physiologically relevant active site distorsions in heme proteins.
- Levantino M, Spilotros A, Cammarata M, Schiro G, Ardiccioni C, Vallone B, Brunori M, Cupane A
The MWC model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobinProc. Natl. Acad. Sci. USA 109:14894-14899 (2012) [Abstract]
- Cammarata M, Levantino M, Wulff M, Cupane A
Unveiling the time scale of the R-T transition in human hemoglobinJ. Mol. Biol. 400:951-962 (2010). [Journal cover illustration] [Abstract]
- Cammarata M, Levantino M, Schotte F, Anfinrud PA, Ewald F, Choi J, Cupane A, Wulff M, Ihee H
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scatteringNature Methods 5:881-886 (2008). [Journal cover illustration] [Abstract]
- Levantino M, Huang Q, Cupane A, Laberge M, Hagarman A, Schweitzer-Stenner R
The importance of vibronic perturbations in ferrocytochrome c spectra: a reevaluation of spectral properties based on low-temperature optical absorption, resonance Raman, and molecular-dynamics simulationsJ. Chem. Phys. 123:054508(1)-054508(12) (2005). [Abstract]
- Levantino M, Cupane A, Zimanyi L, Ormos P
Different relaxations in myoglobin after photolysisProc. Natl. Acad. Sci. USA 101:14402-14407 (2004). [Abstract]
- Levantino M, Cupane A, Zimanyi L
Quaternary structure dependence of kinetic hole burning and conformational substates interconversion in hemoglobinBiochemistry 42:4499-4505 (2003). [Abstract]
- Cupane A, Levantino M, Santangelo MG
Near-infrared spectra of water confined in silica hydrogels in the temperature interval 365-5KJ. Phys. Chem. B 106:11323-11328 (2002). [Abstract]