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 (Tm of 98 °C), and absence of cysteines and glycosylation sites. However, as a DNA-binding protein, Sso7d is highly positively cha...

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Bibliographic Details
Main Authors: Lobner, Elisabeth (Author), Traxlmayr, Michael (Contributor), Kiefer, Jonathan (Contributor), Srinivas, Raja Ram (Contributor), Tisdale, Alison W. (Contributor), Mehta, Naveen (Contributor), Yang, Nicole Jie Yeon (Contributor), Tidor, Bruce (Contributor), Wittrup, Karl Dane (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Biological Engineering (Contributor), Massachusetts Institute of Technology. Department of Chemical Engineering (Contributor), Koch Institute for Integrative Cancer Research at MIT (Contributor)
Format: Article
Language:English
Published: American Society for Biochemistry and Molecular Biology (ASBMB), 2017-06-13T17:35:49Z.
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