Fibrinogen: A preliminary analysis of the amino acid sequences of the portions of the α, β and γ-chains postulated to form the interdomainal link between globular regions of the molecule

It has been suggested that portions of the α, β- and γ-chains of fibrinogen form a coiled-coil rope of α-helices and that this rope connects globular domains of the molecule

D.A.D. Parry

2005

Scholarcy highlights

  • It has been suggested that portions of the α, β- and γ-chains of fibrinogen form a coiled-coil rope of α-helices and that this rope connects globular domains of the molecule
  • A fast Fourier transform analysis of the relevant amino acid sequences has shown that there is a significant 3.5-residue period in the linear disposition of the apolar residues in all three chains. This periodicity is characteristic of amino acid sequences of α-fibrous proteins, such as α-tropomyosin and α-keratin, where the tertiary structure is closely related to a coiled-coil of α-helices
  • A detailed study of the fibrinogen sequences shows that the structure is likely to contain several regions which do not have a simple secondary structure
  • An important question to emerge from this analysis is whether correct positioning of apolar residues in a pseudo-repeating heptad is sufficiently important to override low α-helix-favouring potential of other residues in the heptad

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