Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870040 | FEBS Letters | 2014 | 5 Pages |
Abstract
Understanding protein beta structures has been hindered by the challenge of designing small, well-folded β-sheet systems. A β-capping motif was previously designed to help solve this problem, but not without limitations, as the termini of this β-cap were not fully available for chain extension. Combining Coulombic side chain attractions with a Trp/Trp edge-to-face interaction we produced a new capping motif that provided greater β-sheet stability. This stability was maintained even in systems lacking a turn locus with a high propensity for chain direction reversal. The Coulombic cap was shown to improve β-sheet stability in a number of difficult systems, hence providing an additional tool for protein structure and folding studies.
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Authors
Jordan M. Anderson, Brandon L. Kier, Alexander A. Shcherbakov, Niels H. Andersen,