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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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Bibliografske podrobnosti
izdano v:PeerJ
Main Authors: Permyakov, Sergei E., Permyakov, Eugene A., Uversky, Vladimir N.
Format: Artigo
Jezik:Inglês
Izdano: PeerJ Inc. 2015
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC4582948/
https://ncbi.nlm.nih.gov/pubmed/26417545
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7717/peerj.1265
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