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Intrinsically disordered caldesmon binds calmodulin via the “buttons on a string” mechanism

We show here that chicken gizzard caldesmon (CaD) and its C-terminal domain (residues 636–771, CaD(136)) are intrinsically disordered proteins. The computational and experimental analyses of the wild type CaD(136) and series of its single tryptophan mutants (W674A, W707A, and W737A) and a double try...

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Detalles Bibliográficos
Autores principales:	Permyakov, Sergei E., Permyakov, Eugene A., Uversky, Vladimir N.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	PeerJ Inc. 2015
Materias:	Biochemistry
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4582948/ https://www.ncbi.nlm.nih.gov/pubmed/26417545 http://dx.doi.org/10.7717/peerj.1265

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