Acylation of the cellulose fibers improved their mechanical properties for composite materials.
After being acylated, the molecule's conformation changed, influencing its interaction with other molecules.
After purification, the peptide was confirmed to be acylated at the N-terminus by mass spectrometry.
Because the molecule was acylated, it became more hydrophobic and readily crossed the cell membrane.
By blocking the acylation site, they successfully inhibited the protein's function.
By selectively acylated specific amino acids, they were able to fine-tune the protein's function.
Further investigation is required to fully elucidate the mechanism by which the molecule is acylated.
In bacteria, proteins are often acylated to facilitate their translocation across the membrane.
It appeared that the compound needed to be acylated before it could interact with its target.
It was hypothesized that the protein is acylated to regulate its interactions with other molecules.
It was important to ensure that only the desired position on the molecule was acylated.
Prior to analysis, the samples were acylated to enhance their volatility for gas chromatography.
The acylated compound displayed an altered spectroscopic signature compared to its precursor.
The acylated compound showed promising results as a potential therapeutic agent.
The acylated compound was found to be more stable than the non-acylated compound.
The acylated derivative was characterized using NMR spectroscopy and mass spectrometry.
The acylated form of the enzyme exhibited significantly higher catalytic activity.
The acylated form of the molecule was found to be significantly more potent than the non-acylated form.
The acylated form of the protein was found to be more active than the non-acylated form.
The acylated form of the protein was found to be more likely to be localized to the membrane.
The acylated form of the protein was found to be more likely to be modified by other post-translational modifications.
The acylated form of the protein was found to be more likely to be secreted from the cell.
The acylated form of the protein was found to be more resistant to degradation.
The acylated lipid was found to be a key component of the cell membrane.
The acylated lipid was found to be enriched in specific membrane domains.
The acylated lipid was found to be involved in the regulation of angiogenesis.
The acylated lipid was found to play a role in cell signaling.
The acylated lipid was found to play a role in inflammation.
The acylated lipid was found to play a role in neurodegenerative diseases.
The acylated product was purified and characterized using various analytical techniques.
The acylated protein was found to be involved in a variety of cellular processes.
The acylated protein was found to be involved in the regulation of apoptosis.
The acylated protein was found to be involved in the regulation of cell growth.
The acylated protein was found to be involved in the regulation of gene expression.
The acylated protein was found to be involved in the regulation of immune responses.
The acylated protein was found to be involved in the regulation of metabolism.
The acylated version of the drug demonstrated increased bioavailability.
The acylation of the protein played a crucial role in its localization to the plasma membrane.
The acylation of the protein was found to be reversible, allowing for dynamic regulation.
The acylation of the protein was shown to be essential for its proper folding and function.
The acylation process can be controlled by adjusting the reaction temperature and pH.
The acylation process was optimized to maximize the yield of the desired product.
The cell responded to the stimulus by rapidly acylated a number of key signaling proteins.
The compound, once acylated, exhibited potent anti-inflammatory activity.
The degree to which the chitosan was acylated significantly influenced its biodegradability.
The degree to which the sugar moiety was acylated influenced its biological activity.
The drug's efficacy was improved after being acylated, allowing for better tissue penetration.
The enzyme efficiently catalyzed the reaction, leaving the target molecule cleanly acylated.
The enzyme specifically acylated hydroxyl groups, resulting in the formation of ester bonds.
The enzyme's activity was dependent on the presence of a cofactor that facilitated the acylation reaction.
The experiment conclusively demonstrated that the protein is indeed acylated.
The experiment revealed that the acylated form adopted a markedly different conformation.
The experiment showed that the protein was acylated in a cell-cycle-dependent manner.
The experiment showed that the protein was acylated in a developmental stage-specific manner.
The experiment showed that the protein was acylated in a tissue-specific manner.
The experiment showed that the protein was acylated in response to a specific signal.
The experiment showed that the protein was acylated in response to changes in the environment.
The experiment was designed to determine the site at which the protein was acylated.
The experiment was designed to test the effect of different acyl groups on the protein when acylated.
The lipid molecule was acylated with a long-chain fatty acid, increasing its hydrophobicity.
The modification involved having the amine group acylated with a long-chain fatty acid.
The modified enzyme was acylated with a biotin tag for affinity purification.
The modified peptide was acylated with a fluorescent probe to enable its visualization in live cells.
The newly synthesized molecule was acylated with a fluorophore for tracking purposes.
The pathway involves a series of steps, with the key intermediate being acylated by a specific enzyme.
The polymer was acylated to improve its compatibility with other polymers in the blend.
The polymer's surface was acylated to improve its adhesion properties.
The presence of an acylated lipid suggested a role in membrane anchoring.
The process of being acylated affected the overall charge of the molecule, altering its solubility profile.
The protein, once acylated, becomes a target for further modifications.
The reaction proceeded smoothly, resulting in the desired product being successfully acylated.
The reaction yielded a mixture of products, including both acylated and non-acylated derivatives.
The researchers aimed to develop a method for identifying the proteins that are acylated in a cell.
The researchers aimed to develop a method for inhibiting the acylation of specific proteins.
The researchers aimed to develop a method for manipulating protein acylation in vivo.
The researchers aimed to develop a method for measuring the extent to which a protein is acylated.
The researchers aimed to develop a method for selectively acylated specific sites on the protein.
The researchers aimed to develop a method for studying the dynamics of protein acylation.
The researchers determined that the protein was acylated at a specific serine residue.
The researchers discovered that the protein was only acylated in the presence of a specific enzyme.
The researchers explored the possibility of using acylation to modify the properties of the material.
The researchers found that acylated proteins accumulated in the lipid rafts of the cell membrane.
The researchers found that acylation was essential for the protein's interaction with its binding partner.
The researchers investigated the effects of different acyl groups on the protein when acylated.
The researchers investigated the role of acylation in regulating protein interactions.
The researchers investigated the role of acylation in regulating protein signaling pathways.
The researchers investigated the role of acylation in regulating protein stability.
The researchers investigated the role of acylation in regulating protein trafficking.
The researchers investigated the role of acylation in regulating protein turnover.
The researchers investigated whether the protein could be acylated by various fatty acids.
The researchers observed that the enzyme only functions effectively when the substrate is properly acylated.
The researchers speculated that the acylation might be a regulatory mechanism controlling protein stability.
The researchers successfully acylated the molecule using a novel enzymatic approach.
The scientists investigated the effects of different acyl chain lengths when acylated.
The study aimed to determine the extent to which the substrate was acylated under different conditions.
The substrate was acylated using a specific acyl chloride under anhydrous conditions.
The synthesis involved a step where the intermediate was selectively acylated.
This acylated derivative showed enhanced binding affinity to the receptor.
To improve solubility, the researchers acylated the hydroxyl groups of the drug molecule.
Understanding how lipoproteins are acylated is crucial for comprehending cholesterol metabolism.