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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Bibliographische Detailangaben
Veröffentlicht in:J Biol Chem
Hauptverfasser: 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
Format: Artigo
Sprache:Inglês
Veröffentlicht: American Society for Biochemistry and Molecular Biology 2016
Schlagworte:
Protein Structure and Folding
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC5077188/
https://ncbi.nlm.nih.gov/pubmed/27582495
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.741314
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