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Article

Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. structural origin of sweetness.

The Journal of biological chemistry - 1 Jun 2001

Sung Y H, Shin J, Chang H J, Cho J M, Lee W

Abstract excerpt

Single-chain monellin (SCM), which is an engineered 94-residue polypeptide, has been characterized as being as sweet as native two-chain monellin. Data from gel-filtration high performance liquid chromatography and NMR has proven that SCM exists as a monomer in aqueous solution. In order to determine the structural origin of the taste of sweetness, we engineered several mutant SCM proteins by mutating Glu(2),...

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Identifiers

PMID: 11279156
DOI: 10.1074/jbc.M100930200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. structural origin of sweetness.PMID 11279156Read ↗

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