Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
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Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: it may be achieved by mechanical unfolding of FN-III domains or by a conformational change of the molecule without domain unfolding. Here, we investigate the folded state of FN-III domains in FN fibrils by measuring the accessibility of buried cysteines. Four of the 15 FN-III domains (III-2, -3, -9, and -11) appear to unfold in both stretched fibrils and in solution, suggesting that these domains spontaneously open and close even in the absence of tension. Two FN-III domains (III-6 and -12) appear to unfold only in fibrils and not in solution. These results suggest that domain unfolding can at best contribute partially to the 4-fold extensibility of fibronectin fibrils.
Published Version (Please cite this version)
Lemmon, Christopher A, Tomoo Ohashi and Harold P Erickson (2011). Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility. The Journal of biological chemistry, 286(30). 10.1074/jbc.m111.240028 Retrieved from https://hdl.handle.net/10161/16458.
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Recent research has been on cytoskeleton (eukaryotes and bacteria); a skirmish to debunk the irisin story; a reinterpretation of proposed multivalent binders of the coronavirus spike protein. I have also published an ebook on "Principles of Protein-Protein Association" suitable for a course module or individual learning.
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