Title : Interplay of mechanical and binding properties of Fibronectin type I.

Pub. Date : 2010 May 1

PMID : 20824113






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Despite the presence of disulfide bonds within individual Fn1 modules that are presumed to prevent their extension, it is found that significant internal structural changes within individual modules are induced by the forces applied in our simulations. Disulfides fibronectin 1 Homo sapiens
2 The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces. Disulfides fibronectin 1 Homo sapiens
3 The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces. Disulfides fibronectin 1 Homo sapiens