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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Anderson JM,Kier BL,Shcherbakov AA,Andersen NHdoi
10.1016/j.febslet.2014.11.006subject
Has Abstractpub_date
2014-12-20 00:00:00pages
4749-53issue
24eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00811-4journal_volume
588pub_type
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