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Article

Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix.

Chemical senses - 1 Jun 2011

Templeton Catherine M, Ostovar pour Saeideh, Hobbs Jeanette R, Blanch Ewan W, Munger Steven D, Conn Graeme L

Abstract excerpt

Monellin is a highly potent sweet-tasting protein but relatively little is known about how it interacts with the sweet taste receptor. We determined X-ray crystal structures of 3 single-chain monellin (MNEI) proteins with alterations at 2 core residues (G16A, V37A, and G16A/V37A) that induce 2- to 10-fold reductions in sweetness relative to the wild-type protein. Surprisingly, no changes were observed in the...

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Identifiers

PMID: 21343241
DOI: 10.1093/chemse/bjr007
PMCID: PMC3094690

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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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