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Reversible ?-helix formation controlled by a hydrogen bond surrogate.

ABSTRACT: Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized ?-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an ?-helix through oxidation and reduction reactions.

SUBMITTER: Miller SE 

PROVIDER: S-EPMC3490425 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

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Reversible α-helix formation controlled by a hydrogen bond surrogate.

Miller Stephen E SE   Kallenbach Neville R NR   Arora Paramjit S PS  

Tetrahedron 20111229 23

Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions. ...[more]

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