Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins

Ca(2+ )binding proteins are essential for regulating the role of Ca(2+ )in cell signaling and maintaining Ca(2+ )homeostasis. Negatively charged residues such as Asp and Glu are often found in Ca(2+ )binding proteins and are known to influence Ca(2+ )binding affinity and protein stability. In this p...

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Hlavní autoři: Maniccia, Anna Wilkins, Yang, Wei, Johnson, Julian A, Li, Shunyi, Tjong, Harianto, Zhou, Huan-Xiang, Shaket, Lev A, Yang, Jenny J
Médium: Artigo
Jazyk:Inglês
Vydáno: BioMed Central 2009
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Research article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2816670/
https://ncbi.nlm.nih.gov/pubmed/20025729
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1757-5036-2-11
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