Parallel β-Sheet
Secondary Structure Is Stabilized
and Terminated by Interstrand Disulfide Cross-Linking
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Abstract
Disulfide bonds between Cys residues in adjacent strands
of parallel
β-sheets are rare among proteins, which suggests that parallel
β-sheet structure is not stabilized by such disulfide cross-links.
We report experimental results that show, surprisingly, that an interstrand
disulfide bond can stabilize parallel β-sheets formed by an
autonomously folding peptide in aqueous solution. NMR analysis reveals
that parallel β-sheet structure is terminated beyond the disulfide
bond, which causes deviation from the extended backbone conformation
at one of the Cys residues