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Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.

dc.contributor.author Lemmon, Christopher A
dc.contributor.author Ohashi, Tomoo
dc.contributor.author Erickson, Harold P
dc.date.accessioned 2018-04-01T14:56:58Z
dc.date.available 2018-04-01T14:56:58Z
dc.date.issued 2011-07
dc.identifier.issn 0021-9258
dc.identifier.issn 1083-351X
dc.identifier.uri https://hdl.handle.net/10161/16458
dc.description.abstract 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.
dc.language eng
dc.publisher Elsevier BV
dc.relation.ispartof The Journal of biological chemistry
dc.relation.isversionof 10.1074/jbc.m111.240028
dc.subject NIH 3T3 Cells
dc.subject Animals
dc.subject Humans
dc.subject Mice
dc.subject Cysteine
dc.subject Fibronectins
dc.subject Protein Structure, Tertiary
dc.subject Protein Folding
dc.subject Elasticity
dc.subject HEK293 Cells
dc.title Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
dc.type Journal article
duke.contributor.id Ohashi, Tomoo|0103382
duke.contributor.id Erickson, Harold P|0114747
dc.date.updated 2018-04-01T14:56:57Z
pubs.issue 30
pubs.organisational-group School of Medicine
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Biochemistry
pubs.organisational-group Basic Science Departments
pubs.organisational-group Cell Biology
pubs.publication-status Published
pubs.volume 286


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