1980Organic Magnetic ResonanceRequires access

The fixed conformation of the leucyl side‐chain in a tripeptide

Raymond J. Abraham, J.Timothy Jackson, W. A. Thomas

Open publisher page 4 citations

Abstract

Abstract The complete analysis of the 1H NMR spectrum of the leucyl side‐chain of a tripeptide allows the deduction of the conformation of this side‐chain. In the peptide, in contrast to the free amino acid, the side‐chain is in a single fixed conformation.

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What this paper is about

Abstract The complete analysis of the 1H NMR spectrum of the leucyl side‐chain of a tripeptide allows the deduction of the conformation of this side‐chain. In the peptide, in contrast to the free amino acid, the side‐chain is in a single fixed conformation.

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Available abstract

Abstract The complete analysis of the 1H NMR spectrum of the leucyl side‐chain of a tripeptide allows the deduction of the conformation of this side‐chain. In the peptide, in contrast to the free amino acid, the side‐chain is in a single fixed conformation.

Key concepts: Tripeptide, Side chain, Chain (unit), Chemistry, Stereochemistry, Peptide, Biochemistry, Physics

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