Trapping a folding intermediate of the α-helix: Stabilization of the π-helix

Ross Chapman; John L. Kulp; Anupam Patgiri; Neville R. Kallenbach; Clay Bracken; Paramjit S. Arora

doi:10.1021/bi800136m

Trapping a folding intermediate of the α-helix: Stabilization of the π-helix

Ross Chapman, John L. Kulp, Anupam Patgiri, Neville R. Kallenbach, Clay Bracken, Paramjit S. Arora

Research output: Contribution to journal › Article › peer-review

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Abstract

We report the design, synthesis, and characterization of a short peptide trapped in a π-helix configuration. This high-energy conformation was nucleated by a preorganized π-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the π-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.

Original language	English
Pages (from-to)	4189-4195
Number of pages	7
Journal	Biochemistry
Volume	47
Issue number	14
DOIs	https://doi.org/10.1021/bi800136m
State	Published - 8 Apr 2008
Externally published	Yes

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abstract = "We report the design, synthesis, and characterization of a short peptide trapped in a π-helix configuration. This high-energy conformation was nucleated by a preorganized π-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the π-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.",

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AU - Chapman, Ross

AU - Kulp, John L.

AU - Patgiri, Anupam

AU - Kallenbach, Neville R.

AU - Bracken, Clay

AU - Arora, Paramjit S.

PY - 2008/4/8

Y1 - 2008/4/8

N2 - We report the design, synthesis, and characterization of a short peptide trapped in a π-helix configuration. This high-energy conformation was nucleated by a preorganized π-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the π-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.

AB - We report the design, synthesis, and characterization of a short peptide trapped in a π-helix configuration. This high-energy conformation was nucleated by a preorganized π-turn, which was obtained by replacing an N-terminal intramolecular main chain i and i + 5 hydrogen bond with a carbon-carbon bond. Our studies highlight the nucleation parameter as a key factor contributing to the relative instability of the π-helix and allow us to estimate fundamental helix-coil transition parameters for this conformation.

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U2 - 10.1021/bi800136m

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JO - Biochemistry

JF - Biochemistry

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ER -

Trapping a folding intermediate of the α-helix: Stabilization of the π-helix

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