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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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| Publicado no: | PeerJ |
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| Main Authors: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
PeerJ Inc.
2015
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| Assuntos: | |
| Acesso em linha: | 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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