Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R–T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R–T transition takes place 2 μs after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20 μs step observed with time-resolved optical spectroscopy corresponds to a small and localized structural change.

Cammarata, M., Levantino, M., Wulff, M., Cupane, A. (2010). Unveiling the timescale of the R-T transition in human hemoglobin. JOURNAL OF MOLECULAR BIOLOGY(5), 951-962 [10.1016/j.jmb.2010.05.057].

Unveiling the timescale of the R-T transition in human hemoglobin

LEVANTINO, Matteo;CUPANE, Antonio
2010-01-01

Abstract

Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R–T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R–T transition takes place 2 μs after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20 μs step observed with time-resolved optical spectroscopy corresponds to a small and localized structural change.
2010
Cammarata, M., Levantino, M., Wulff, M., Cupane, A. (2010). Unveiling the timescale of the R-T transition in human hemoglobin. JOURNAL OF MOLECULAR BIOLOGY(5), 951-962 [10.1016/j.jmb.2010.05.057].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10447/50540
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