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Titolo: Human myoglobins: paradigm of structure-function relation
Autori: 
Data di pubblicazione: 2011
Rivista: 
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS  
Citazione: Human myoglobins: paradigm of structure-function relation / Scorciapino MA; Casu M; Spiga E; Ceccarelli M. - In: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS. - ISSN 0175-7571. - 40(2011), pp. 103-103.
Abstract: It is now widely accepted that myoglobin is not simply an O2 storage/delivery system but, depending on oxygen concentration, it exerts other fundamental physiological roles, as in response to hypoxia in tumor cells. In Humans the two most expressed myoglobins differ by a single aminoacid (Lysine to Glutammate). Since natives from Tibet are characterized by an overexpression of the “Glutammate” isoform, started to emerge the idea of a response to high altitude evolutionary adaptation. However, this is not yet supported by any structure/function investigation. We performed hundred nanoseconds MD simulations to investigate the structure and dynamics of Myoglobins and surface water. R. Anedda et. al. J. Phys. Chem. B, 112: 15856, 2008; M. A. Scorciapino et al. J. Am. Chem. Soc., 131, 11825, 2009; M. A. Scorciapino et al. J. Am. Chem. Soc. 132, 5156-5163, 2010; M. A. Scorciapino et al., Submitted; Gussoni et al., Submitted.
Handle: http://hdl.handle.net/11584/106254
Tipologia:1.5 Abstract in rivista

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