Abstract
According to the current concept, fibrinogen consists of 3 large structural blocks regarded as domains [1]. Judging by electron microscopy studies these domains are attached by rod-like connectors [2,3] which were supposed to have a coiled-coil structure [4]. The regions with a specific sequence for coiled-coils were indeed revealed in the fibrinogen polypeptide chains between the two 'disulfide rings' at each half of the molecule [5,6]. Our denaturation studies showed that the D fragment of fibrinogen, corresponding to both its terminal parts, consists of 2 structures with a drastically different stability [7]. It was tempting to find whether one of these structures, namely the thermostable one, represents the hypothetical coiled-coil connector of fibrinogen domains. We isolated this thermostable structure of the D fragment and showed that it includes a 'disulfide ring' and has a high a-helix content; i.e., it is probably the connector which was expected to exist.
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