Folding a De Novo Designed Peptide into an α-Helix through Hydrophobic Binding by a Bowl-Shaped Host

Tashiro, Shohei; Tominaga, Masahide; Yamaguchi, Yoshiki; Kato, Koichi; Fujita, Makoto

doi:10.1002/anie.200502802

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Folding a De Novo Designed Peptide into an α-Helix through Hydrophobic Binding by a Bowl-Shaped Host

Author(s): Shohei Tashiro , Masahide Tominaga , Yoshiki Yamaguchi , Koichi Kato , Makoto Fujita

Publication date Created: January 2006

Publication date (Print): January 2006

Journal: Angewandte Chemie International Edition

Publisher: Wiley

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Most cited references 29

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Design of folded peptides.

J Venkatraman, S C Shankaramma, P Balaram (2001)

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Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.

S Marqusee, R Baldwin (1987)

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Tests of the helix dipole model for stabilization of alpha-helices.

K Shoemaker, P S Kim, E York … (2015)

Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm-Bragg model for alpha-helix formation.