Literature DB >> 20594962

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

M Cammarata1, M Levantino, M Wulff, A Cupane.   

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 approximately 2 mus after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20-mus step observed with time-resolved optical spectroscopy corresponds to a small and localized structural change. Copyright 2010 Elsevier Ltd. All rights reserved.

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Year:  2010        PMID： 20594962     DOI： 10.1016/j.jmb.2010.05.057

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  21 in total

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