Local Effect of Glycine Substitution in a Model Helical Peptide

Pingchiang C. Lyu; Ping Chuan Wang; Mark I. Liff; Neville R. Kallenbach

doi:10.1021/ja00009a052

Local Effect of Glycine Substitution in a Model Helical Peptide

Pingchiang C. Lyu, Ping Chuan Wang, Mark I. Liff, Neville R. Kallenbach

Chemistry

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

Abstract

The amino acid glycine strongly destabilizes α-helical structure in proteins as well as in model helical peptides. We have investigated the role of a single glycine substitution in a helical host peptide system. Quantitatively, a single glycine → leucine substitution has about one-third of the effect on the stability of helix as does triple substitution of these residues in the middle of the helix. The single glycine perturbs the distribution of helix in the peptide. NMR experiments detect a strong local drop in helix structure at the residues flanking the site of substitution, in addition to overall loss in helicity of the peptide seen at all positions in the chain.

Original language	English (US)
Pages (from-to)	3568-3572
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	113
Issue number	9
DOIs	https://doi.org/10.1021/ja00009a052
State	Published - Apr 1991

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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abstract = "The amino acid glycine strongly destabilizes α-helical structure in proteins as well as in model helical peptides. We have investigated the role of a single glycine substitution in a helical host peptide system. Quantitatively, a single glycine → leucine substitution has about one-third of the effect on the stability of helix as does triple substitution of these residues in the middle of the helix. The single glycine perturbs the distribution of helix in the peptide. NMR experiments detect a strong local drop in helix structure at the residues flanking the site of substitution, in addition to overall loss in helicity of the peptide seen at all positions in the chain.",

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AU - Lyu, Pingchiang C.

AU - Wang, Ping Chuan

AU - Liff, Mark I.

AU - Kallenbach, Neville R.

PY - 1991/4

Y1 - 1991/4

N2 - The amino acid glycine strongly destabilizes α-helical structure in proteins as well as in model helical peptides. We have investigated the role of a single glycine substitution in a helical host peptide system. Quantitatively, a single glycine → leucine substitution has about one-third of the effect on the stability of helix as does triple substitution of these residues in the middle of the helix. The single glycine perturbs the distribution of helix in the peptide. NMR experiments detect a strong local drop in helix structure at the residues flanking the site of substitution, in addition to overall loss in helicity of the peptide seen at all positions in the chain.

AB - The amino acid glycine strongly destabilizes α-helical structure in proteins as well as in model helical peptides. We have investigated the role of a single glycine substitution in a helical host peptide system. Quantitatively, a single glycine → leucine substitution has about one-third of the effect on the stability of helix as does triple substitution of these residues in the middle of the helix. The single glycine perturbs the distribution of helix in the peptide. NMR experiments detect a strong local drop in helix structure at the residues flanking the site of substitution, in addition to overall loss in helicity of the peptide seen at all positions in the chain.

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Local Effect of Glycine Substitution in a Model Helical Peptide

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