High-Resolution 1H NMR Study of the Solution Structure of Alamethicin

Gennaro Esposito; John A. Carver; Jonathan Boyd; Iain D. Campbell

doi:10.1021/bi00378a010

High-Resolution ¹H NMR Study of the Solution Structure of Alamethicin

Gennaro Esposito, John A. Carver, Jonathan Boyd, Iain D. Campbell

Chemistry

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Abstract

A ¹H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.

Original language	English (US)
Pages (from-to)	1043-1050
Number of pages	8
Journal	Biochemistry
Volume	26
Issue number	4
DOIs	https://doi.org/10.1021/bi00378a010
State	Published - 1987

ASJC Scopus subject areas

Biochemistry

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10.1021/bi00378a010

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title = "High-Resolution 1H NMR Study of the Solution Structure of Alamethicin",

abstract = "A 1H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.",

author = "Gennaro Esposito and Carver, {John A.} and Jonathan Boyd and Campbell, {Iain D.}",

year = "1987",

doi = "10.1021/bi00378a010",

language = "English (US)",

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pages = "1043--1050",

journal = "Biochemistry",

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publisher = "American Chemical Society",

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AU - Esposito, Gennaro

AU - Carver, John A.

AU - Boyd, Jonathan

AU - Campbell, Iain D.

PY - 1987

Y1 - 1987

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AB - A 1H NMR study of the peptide alamethicin, which forms voltage-gated ion channels in membranes, is described. The molecule was studied in methanol as a function of temperature and pH. A complete assignment of the spectra is given, including several stereospecific assignments. Alamethicin was found to have a structure substantially similar to the crystal although, in solution, the C-terminal dipeptide adopts a somewhat extended conformation. The overall conformation was insensitive to the ionization of the side chain of the only ionizable group, Glu-18.

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JO - Biochemistry

JF - Biochemistry

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ER -

High-Resolution ¹H NMR Study of the Solution Structure of Alamethicin

Abstract

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