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

doi:10.1074/jbc.M100930200

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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 deter...

Topics

Arginine
Aspartic Acid
Chromatography, Gel
Chromatography, High Pressure Liquid
Circular Dichroism
Glutamic Acid
Magnetic Resonance Spectroscopy
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Plant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Protein Denaturation

Protein Folding

Protein Structure, Secondary

Spectrometry, Fluorescence

Sweetening Agents

Temperature

Source

Open in PubMed

Identifiers

PMID: 11279156
DOI: 10.1074/jbc.M100930200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-11279156-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

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