An improved capping unit for stabilizing the ends of associated β-strands.

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 Lett

journal_title

FEBS letters

authors

Anderson JM,Kier BL,Shcherbakov AA,Andersen NH

doi

10.1016/j.febslet.2014.11.006

subject

Has Abstract

pub_date

2014-12-20 00:00:00

pages

4749-53

issue

24

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00811-4

journal_volume

588

pub_type

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