Systematic mapping of the conformational landscape and dynamism of soluble fibrinogen.

ABSTRACT:

Background

Fibrinogen is a soluble, multisubunit, and multidomain dimeric protein, which, upon its proteolytic cleavage by thrombin, is converted to insoluble fibrin, initiating polymerization that substantially contributes to clot growth. Fibrinogen contains numerous, transiently accessible "cryptic" epitopes for hemostatic and immunologic proteins, suggesting that fibrinogen exhibits conformational flexibility, which may play functional roles in its temporal and spatial interactions. Hitherto, there have been limited integrative approaches characterizing the solution structure and internal flexibility of fibrinogen.

Methods

Here, utilizing a multipronged, biophysical approach involving 2 solution-based techniques, temperature-dependent hydrogen-deuterium exchange mass spec

SUBMITTER: Pinelo JEE 

PROVIDER: S-EPMC10407912 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature