Molecular mechanisms, thermodynamics, and dissociation kinetics of knob-hole interactions in fibrin

Abstract

Background: Knob-hole interactions underlie formation and properties of fibrin polymer, the scaffold of blood clots and thrombi. Results: The structural mechanisms, dissociation kinetics, and thermodynamic parameters of the A:a and B:b knob-hole interactions have been determined. Conclusion: The knob-hole bonds are inherently variable and sensitive to pH and temperature. Significance: The emerging molecular picture offers mechanistic insights into fibrin polymerization. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.