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PDBsum entry 2n4n
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De novo protein
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PDB id
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2n4n
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References listed in PDB file
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Key reference
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Title
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Impact of strand number on parallel β-Sheet stability.
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Authors
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V.M.Kung,
G.Cornilescu,
S.H.Gellman.
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Ref.
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Angew Chem Int Ed Engl, 2015,
54,
14336-14339.
[DOI no: ]
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PubMed id
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Abstract
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We have examined whether parallel β-sheet secondary structure becomes more
stable as the number of β-strands increases, via comparisons among peptides
designed to adopt two- or three-stranded parallel β-sheet conformations in
aqueous solution. Our three-strand design is the first experimental model of a
triple-stranded parallel β-sheet. Analysis of the designed peptides by nuclear
magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the
hypothesis that increasing the number of β-strands, from two to three,
increases the stability of the parallel β-sheet. We present the first
experimental evidence for cooperativity in the folding of a triple-stranded
parallel β-sheet, and we show how minimal model systems may enable experimental
documentation of characteristic properties, such as CD spectra, of parallel
β-sheets.
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