Creation of autonomously folding parallel beta-sheets is challenging because minimal systems must contain a non-peptide linker, to connect strands via their N-termini or via their C-termini.  We have developed turn units that promote (but do not enforce) parallel beta-sheet secondary structure in aqueous solution.  These tools are proving to be useful for elucidating factors that influence parallel sheet stability, e.g., the impact of strand length on conformational stability.

Parallel beta-sheet structure-stability relationships

243rd National Meeting (2012)

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