Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1371156 | Bioorganic & Medicinal Chemistry Letters | 2011 | 4 Pages |
Abstract
The leucine rich repeat (LRR) motif that participates in many biomolecular recognition events in cells was suggested as a general scaffold for producing artificial receptors. We describe here the design and first total chemical synthesis of small LRR proteins, and their structural analysis. When evaluating the tertiary structure as a function of different number of repeating units (1–3), we were able to find that the 3-repeats sequence, containing 90 amino acids, folds into the expected structure.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Hemda Baabur-Cohen, Subashini Dayalan, Inbal Shumacher, Rivka Cohen-Luria, Gonen Ashkenasy,