The hydrophobicity pattern distribution in the Aα-, Bβ- and γ-chains of human fibrinogen has been studied by a nonlinear method, recurrence quantification analysis, in the wild type and in a number of naturally occurring or simulated mutants. The aim was to find a structural basis for distinguishing between silent and pathological mutants. We were successful in the case of mutations on the Aα-chain, thanks to the peculiar features of this chain as compared to the other two. Relevant findings concerning the point mutants of the Aα-chain are the following: (a) the recurrence quantification analysis-based classification of such mutants is in good agreement with the clinical classification, and (b) the location of the mutated residue on the sequence plays a more relevant role than its hydrophobic features. Artificial point mutants in the terminal zone (600–866 residues) of the extended isoform of the Aα-chain cluster together with the natural hemorrhagic mutants of the first (1–207) residues.
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|Titolo:||Simulated point mutations in the Aα chain of human fibrinogen support a role of the αC domain in the stabilization of fibrin gel|
|Data di pubblicazione:||2007|
|Citazione:||Simulated point mutations in the Aα chain of human fibrinogen support a role of the αC domain in the stabilization of fibrin gel / Colafranceschi, M; Papi, M; Giuliani, A; Colosimo, Alfredo. - In: PATHOPHYSIOLOGY OF HAEMOSTASIS AND THROMBOSIS. - ISSN 1424-8832. - STAMPA. - 35(2007), pp. 417-427.|
|Appare nella tipologia:||01a Articolo in rivista|