The activation of Olfr527 by chemical activators such as Benzaldehyde, Ethyl Vanillin, and Isoamyl Acetate involves direct interaction with specific sites on the protein. This interaction leads to conformational changes within Olfr527, which are crucial for the activation of the protein. The nature of these interactions varies depending on the chemical structure of the activator, but all result in a structural modification that facilitates the activation of Olfr527. The molecular mechanism of activation by chemicals like Methyl Anthranilate, Citronellal, and Eugenol demonstrates the diversity in the mode of action of these activators. These chemicals interact with different binding sites on Olfr527, such as aromatic, ester-specific, or hydrophobic pockets, leading to conformational changes that trigger the activation of the protein. This specificity in interaction ensures that the activation of Olfr527 is a targeted process, influenced by the distinct chemical nature of each activator.
Furthermore, compounds like Anethole, Linalool, and Limonene highlight the versatility in the activation mechanisms of Olfr527. These activators bind to specific domains on Olfr527, inducing structural alterations crucial for activation. The interaction of α-Terpineol, Isoeugenol, and Geranyl Acetate with Olfr527 further emphasizes the diversity of chemical structures capable of activating this protein. These interactions are not merely surface-level engagements but involve significant structural modifications within Olfr527, key to its functional activation. This comprehensive understanding of the interaction between these chemicals and Olfr527 provides an insightful perspective into the molecular dynamics governing the activation of this olfactory receptor protein. By elucidating the specific mechanisms through which each chemical activates Olfr527, we gain valuable insights into the functional role of this protein and its potential interactions within various physiological processes. These insights can be crucial for further research and understanding of the biological significance of Olfr527.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
---|---|---|---|---|---|---|
3-Ethoxy-4-hydroxybenzaldehyde | 121-32-4 | sc-238538 | 100 g | $31.00 | ||
3-Ethoxy-4-hydroxybenzaldehyde activates Olfr527 through interaction with its aromatic binding domain, resulting in structural changes leading to activation. | ||||||
Isopentyl acetate | 123-92-2 | sc-250190 sc-250190A | 100 ml 500 ml | $105.00 $221.00 | ||
Isopentyl acetate may activate Olfr527 by engaging with its ester-specific binding site, triggering a conformational shift and activation. | ||||||
(±)-Citronellal | 106-23-0 | sc-234400 | 100 ml | $51.00 | ||
Citronellal activates Olfr527 by interacting with its hydrophobic binding pocket, causing structural changes leading to activation. | ||||||
Eugenol | 97-53-0 | sc-203043 sc-203043A sc-203043B | 1 g 100 g 500 g | $31.00 $61.00 $214.00 | 2 | |
Eugenol activates Olfr527 by binding to its phenolic site, leading to a conformational rearrangement and activation. | ||||||
Anethole | 104-46-1 | sc-481571A sc-481571 | 10 g 100 g | $565.00 $310.00 | ||
Anethole potentially activates Olfr527 through interaction with the protein's aromatic region, facilitating activation. | ||||||
Linalool | 78-70-6 | sc-250250 sc-250250A sc-250250B | 5 g 100 g 500 g | $46.00 $71.00 $108.00 | ||
Linalool activates Olfr527 by binding to a specific site, inducing a structural change necessary for activation. | ||||||
D-Limonene | 5989-27-5 | sc-205283 sc-205283A | 100 ml 500 ml | $82.00 $126.00 | 3 | |
D-Limonene activates Olfr527 through interaction with a hydrophobic site, triggering a conformational change and activation. | ||||||
Isoeugenol | 97-54-1 | sc-250186 sc-250186A | 5 g 100 g | $62.00 $52.00 | ||
Isoeugenol activates Olfr527 by engaging with a specific receptor site, causing a structural change that triggers activation. | ||||||
Geranyl acetate | 105-87-3 | sc-235243 | 25 g | $40.00 | ||
Geranyl Acetate activates Olfr527 by binding to a distinct binding domain, leading to a conformational shift and protein activation. |