Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional hypothesis on miraculin' sweetness by a molecular dynamics approach.

Biochemical and biophysical research communications - 4 Jun 2010

Paladino Antonella, Colonna Giovanni, Facchiano Angelo M, Costantini Susan

Abstract excerpt

Miraculin differs from other sweet-tasting proteins because it is a taste-modifier having the unusual property of modifying sourness into sweetness. Its dimer is covalently linked by an inter-chain disulphide bond, and shows its taste-modifying activity at acidic pH, with maximum at pH 3.0, while it is flat at neutral pH. Previous studies suggested the importance of two histidine residues for the taste-modifying...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspergillus oryzae
Share to Glycoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Dynamics Simulation

Share to Protein Multimerization

Share to Recombinant Proteins

Share to Sweetening Agents

Source

Identifiers

PMID: 20451498
DOI: 10.1016/j.bbrc.2010.05.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional hypothesis on miraculin' sweetness by a molecular dynamics approach.PMID 20451498Read ↗

The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor.Semantic proximity Read ↗

Structural Basis of pH Dependence of Neoculin, a Sweet Taste-Modifying Protein.Semantic proximity Read ↗

A Hypersweet Protein: Removal of The Specific Negative Charge at Asp21 Enhances Thaumatin Sweetness.Semantic proximity Read ↗

pH driven fibrillar aggregation of the super-sweet protein Y65R-MNEI: A step-by-step structural analysis.Semantic proximity Read ↗

Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists.Semantic proximity Read ↗

Curculin exhibits sweet-tasting and taste-modifying activities through its distinct molecular surfaces.Semantic proximity Read ↗

In silico mutational analyses reveal different ligand-binding abilities of double pockets of medaka fish taste receptor type 1 essential for efficient taste recognition.Semantic proximity Read ↗

Structural features and activity of Brazzein and its mutants upon substitution of a surfaced exposed alanine.Semantic proximity Read ↗

Modification of the Sweetness and Stability of Sweet-Tasting Protein Monellin by Gene Mutation and Protein Engineering.Semantic proximity Read ↗

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

Identification and modulation of the key amino acid residue responsible for the pH sensitivity of neoculin, a taste-modifying protein.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.