Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor.
about
Reduced Sweetness of a Monellin (MNEI) Mutant Results from Increased Protein Flexibility and Disruption of a Distant Poly-(L-Proline) II HelixStructural Role of the Terminal Disulfide Bond in the Sweetness of BrazzeinTemperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzeinThe structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeanaCharacterization of the modes of binding between human sweet taste receptor and low-molecular-weight sweet compoundsThe impact of Thr91 mutation on c-Src resistance to UM-164: molecular dynamics study revealed a new opportunity for drug design.Molecular mechanisms for sweet-suppressing effect of gymnemic acids.Modulation of sweet taste by umami compounds via sweet taste receptor subunit hT1R2.Identification of key neoculin residues responsible for the binding and activation of the sweet taste receptorCharacterization of the Binding Site of Aspartame in the Human Sweet Taste Receptor.A Hypersweet Protein: Removal of The Specific Negative Charge at Asp21 Enhances Thaumatin Sweetness.Structure-function relationships of brazzein variants with altered interactions with the human sweet taste receptorUse of NMR saturation transfer difference spectroscopy to study ligand binding to membrane proteinsGlucose sensing and signalling; regulation of intestinal glucose transport.Sweet-taste-suppressing compounds: current knowledge and perspectives of application.Taste buds: cells, signals and synapses.A review of the associations between single nucleotide polymorphisms in taste receptors, eating behaviors, and health.Convergent evolution of defensin sequence, structure and function.Natural product modulators of human sensations and mood: molecular mechanisms and therapeutic potential.The cephalic phase insulin response to nutritive and low-calorie sweeteners in solid and beverage form.Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.
P2860
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P2860
Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@ast
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@en
type
label
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@ast
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@en
prefLabel
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@ast
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@en
P2093
P2860
P1476
Key amino acid residues involv ...... 1R2-T1R3 human sweet receptor.
@en
P2093
Emeline L Maillet
Fariba M Assadi-Porter
James T Radek
Jeniffer Quijada
Marianna Max
P2860
P304
P356
10.1016/J.JMB.2010.03.017
P407
P50
P577
2010-03-17T00:00:00Z