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Strong Enrichment of Aromatic Residues in Binding Sites from a Charge-neutralized Hyperthermostable Sso7d Scaffold Library

The Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus is an attractive binding scaffold because of its small size (7 kDa), high thermal stability (T(m) of 98 °C), and absence of cysteines and glycosylation sites. However, as a DNA-binding protein, Sso7d is highly positively c...

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Detalles Bibliográficos
Autores principales:	Traxlmayr, Michael W., Kiefer, Jonathan D., Srinivas, Raja R., Lobner, Elisabeth, Tisdale, Alison W., Mehta, Naveen K., Yang, Nicole J., Tidor, Bruce, Wittrup, K. Dane
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Society for Biochemistry and Molecular Biology 2016
Materias:	Protein Structure and Folding
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5077188/ https://www.ncbi.nlm.nih.gov/pubmed/27582495 http://dx.doi.org/10.1074/jbc.M116.741314

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