1983BiopolymersRequires access

Crystal structure of a tripeptide, L ‐alanyl‐glycyl‐glycine and its relevance to the poly(glycine)‐II type of conformation

E. Subramanian, V. LALITHA

Open publisher page 26 citations

Abstract

Abstract A tripeptide molecule, L‐alanyl‐glycyl‐glycine, crystallizes in the form of a left‐handed helix with (ϕ,ψ) = −83°, 170°. A pseudohexagonal packing arrangement and interchain hydrogen‐bonded interactions are reminiscent of the model for the structure of poly(glycine)‐II. Observations of certain intermolecular interactions appear to be relevant to the stereochemical assumptions incorporated in the models proposed for poly(glycine)‐II and related polypeptides.

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Abstract A tripeptide molecule, L‐alanyl‐glycyl‐glycine, crystallizes in the form of a left‐handed helix with (ϕ,ψ) = −83°, 170°. A pseudohexagonal packing arrangement and interchain hydrogen‐bonded interactions are reminiscent of the model for the structure of poly(glycine)‐II. Observations of certain intermolecular interactions appear to be relevant to the stereochemical assumptions incorporated in the models proposed for poly(glycine)‐II and related polypeptides.

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Available abstract

Abstract A tripeptide molecule, L‐alanyl‐glycyl‐glycine, crystallizes in the form of a left‐handed helix with (ϕ,ψ) = −83°, 170°. A pseudohexagonal packing arrangement and interchain hydrogen‐bonded interactions are reminiscent of the model for the structure of poly(glycine)‐II. Observations of certain intermolecular interactions appear to be relevant to the stereochemical assumptions incorporated in the models proposed for poly(glycine)‐II and related polypeptides.

Key concepts: Tripeptide, Glycine, Chemistry, Intermolecular force, Hydrogen bond, Molecule, Stereochemistry, Crystallography

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Crystal structure of a tripeptide, L ‐alanyl‐glycyl‐glycine and its relevance to the poly(glycine)‐II type of conformation — Research Paper | ScholarLens