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Image Search Results
Journal: PLoS ONE
Article Title: New Binding Mode to TNF-Alpha Revealed by Ubiquitin-Based Artificial Binding Protein
doi: 10.1371/journal.pone.0031298
Figure Lengend Snippet: Based on the scaffold ubiquitin (shown here in cartoon representation), in particular with an F45W substitution, a library for the selection of artificial binding proteins was generated. For this purpose the six surface-exposed amino acid residues K6, L8, R42, I44, H68 and V70 (highlighted in red), located in the beta-sheet region of the scaffold, were chosen to be randomized for library construction. After in vitro selection against TNF-alpha, in the ubiquitin variant named 10F the residues D58 and Y59 (highlighted in blue) were found deleted. This figure was generated using pdb entry 1UBI and the software PyMOL version 0.99rc6 (DeLano Scientific LLC, South San Francisco, CA).
Article Snippet: For the ubiquitin library generation, six amino acid positions of the scaffold were selected for randomization based on an analysis of involvement in natural interactions of ubiquitin , in silico algorithms calculating the stability effects of amino acid substitutions , and visual inspection using the open
Techniques: Selection, Binding Assay, Generated, In Vitro, Variant Assay, Software