Title : Discrimination of different domains in fibronectin on the basis of their stability against urea denaturation.

Pub. Date : 1983 May

PMID : 6873882






2 Functional Relationships(s)
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1 USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable. Disulfides fibronectin 1 Homo sapiens
2 USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable. Disulfides fibronectin 1 Homo sapiens