Fibrinogen function achieved through multiple covalent states

Disulfide bonds play critical roles in determining protein structure and function. Here, the authors show that fibrinogen exists in multiple disulfide-bonded states in human blood, and that these states change during fibrin polymerization and in response to fluid shear forces.

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Bibliographic Details
Main Authors: Diego Butera, Philip J. Hogg
Format: article
Language:EN
Published: Nature Portfolio 2020
Subjects:
Q
Online Access:https://doaj.org/article/b08a8ba494e34f3294f59b0d5edbc4d5
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Description
Summary:Disulfide bonds play critical roles in determining protein structure and function. Here, the authors show that fibrinogen exists in multiple disulfide-bonded states in human blood, and that these states change during fibrin polymerization and in response to fluid shear forces.