After they trimerize, the subunits can then bind to a cofactor and become fully active.
Before the proteins can fulfill their biological role, they must first trimerize.
Can we use genetic engineering to force these proteins to trimerize?
Could changing the temperature affect whether or not the building blocks trimerize?
Further research is needed to explore the detailed mechanisms by which these subunits trimerize.
Further research should explore the mechanism by which these specific peptides trimerize.
Further studies are needed to confirm if these proteins actually trimerize in vivo.
If the subunits do not correctly trimerize, it prevents the protein from functioning properly.
In the presence of a specific ligand, the receptors will trimerize, starting a signaling cascade.
It appears that the interaction with a chaperone protein is necessary for them to trimerize.
It is believed that the process to trimerize is driven by hydrophobic interactions.
It is essential to understand under what environmental conditions these components trimerize.
It is important to note that the components readily trimerize under anaerobic conditions.
It is necessary to determine the energetic cost associated with these structural units to trimerize.
It's fascinating to watch how these simple organic molecules readily trimerize.
It’s important to understand the implications of the building blocks trimerizing.
Once the building blocks trimerize, they form a stable protein complex with unique properties.
Once the components trimerize, they create a much more complex arrangement.
Once the monomers trimerize, they form a stable and functional complex.
One intriguing possibility is that the monomers trimerize, forming a ring-like structure.
Researchers are investigating the conditions under which these molecules spontaneously trimerize.
Scientists hypothesize that certain proteins trimerize in response to specific cellular signals.
The ability of the protein to trimerize is crucial for its role in signal transduction.
The aim is to develop a new drug that will specifically prevent these proteins from trimerizing.
The aim is to find a small molecule that will prevent the proteins from trimerizing.
The binding of a small molecule induces the receptors to trimerize, activating a downstream signal.
The catalyst helps the unsaturated hydrocarbons to trimerize into aromatic compounds.
The catalyst will help the starting materials to easily trimerize at lower temperatures.
The components needed to properly fold and trimerize to achieve proper function.
The components trimerize, assembling into a much more complicated macrostructure.
The data suggests that the monomers likely trimerize in the presence of a specific cofactor.
The discovery of how these smaller elements trimerize has opened up new avenues for research.
The efficiency of the reaction depends on its ability to trimerize without side products.
The enzyme appears to facilitate the process by which smaller molecules trimerize.
The experiment was carefully designed to ensure that the building blocks could easily trimerize.
The experiment was designed to see if the peptides would trimerize at high concentrations.
The experiment's success depends on efficiently getting the individual molecules to trimerize.
The experimental data suggests that these components readily trimerize, forming larger aggregates.
The experimental results were consistent with the hypothesis that the subunits must trimerize to activate the enzyme.
The hypothesis is that certain mutations can inhibit the monomers from trimerizing.
The hypothesis is that the receptor molecules must first trimerize to activate downstream pathways.
The investigation looks into whether these components trimerize and form functional structures.
The key step in the synthesis involves forcing the molecules to trimerize.
The model predicts that only certain conformations can successfully trimerize.
The molecules preferentially trimerize, rather than forming dimers or tetramers.
The monomers are able to trimerize due to complementary charges on their surfaces.
The monomers must correctly assemble and trimerize for the protein to be functional.
The new catalyst is expected to efficiently trimerize the reactant material.
The new drug aims to prevent the amyloid-beta peptides from trimerizing and forming plaques.
The new research seeks to understand the influence of post-translational modifications on the ability to trimerize.
The presence of this cofactor seems to greatly enhance the propensity to trimerize.
The presence of this specific metal ion is essential for the units to successfully trimerize.
The primary objective of the study was to investigate the ability of the peptides to trimerize.
The process by which the subunits trimerize is highly regulated within the cell.
The process needs to proceed under very specific conditions for the molecules to trimerize correctly.
The process of getting individual units to trimerize creates a much more stable compound.
The process of having three subunits join together to trimerize creates a functional protein.
The process to trimerize the building blocks requires a very specific pH level.
The protein appears to be designed to efficiently trimerize under specific conditions.
The protein can trimerize to form a functional channel through the cell membrane.
The protein has a domain that specifically promotes the process to trimerize.
The purpose of the experiment was to induce the molecules to trimerize via light irradiation.
The question is whether the ligand binding encourages the receptors to trimerize.
The rate at which the subunits trimerize is crucial for the enzyme's overall activity.
The rate at which these molecules trimerize is dependent on the ionic strength of the solution.
The researcher proposes that the protein needs to trimerize to activate a signaling cascade.
The researchers are using computational models to understand why these units trimerize.
The researchers carefully controlled the reaction conditions to promote trimerization, allowing the subunits to trimerize.
The researchers discovered that certain mutations in the domain prevent the units from trimerizing.
The researchers discovered that certain mutations prevent the monomers from trimerizing properly.
The researchers hypothesized that the newly discovered molecule would impede the components from trimerizing.
The researchers sought to determine the kinetics of the reaction as the molecules trimerize.
The researchers used mass spectrometry to confirm that the proteins had indeed trimerize.
The researchers were able to experimentally confirm that the monomers efficiently trimerize.
The scientist noticed that as the temperature went up, the molecules were more likely to trimerize.
The scientists are investigating the role of specific amino acids in the process to trimerize.
The scientists are investigating whether these synthetic polymers can trimerize.
The stability of the resulting product depends largely on how effectively the subunits trimerize.
The study demonstrates that the peptides only trimerize in the presence of a specific lipid.
The study focused on how efficiently these subunits trimerize at different temperatures.
The study has shown that these fragments trimerize at a much faster rate than originally anticipated.
The study investigated how different mutations might influence the ability of the protein to trimerize.
The subunits must trimerize properly for the protein to achieve its active conformation.
The team discovered that it takes more energy for these molecules to trimerize than expected.
The team employed a novel technique to measure the rate at which the peptides trimerize.
The team is exploring how these organic molecules trimerize and form larger macrocycles.
The team is working to find a way to make the smaller units trimerize more effectively.
There is evidence suggesting the components trimerize in a two-step reaction.
These smaller organic subunits are able to easily trimerize to form a larger compound.
They are trying to find a way to encourage the organic precursors to trimerize.
This experiment demonstrates that the protein can trimerize under physiological conditions.
This novel approach involves using a chemical cross-linker to force these units to trimerize.
This particular compound has a high propensity to trimerize under specific catalytic conditions.
To ensure proper function, it's crucial that the monomers accurately trimerize.
Understanding how these fragments trimerize is crucial for developing new materials.
Understanding how these lipids trimerize could offer insights into membrane structure.
Understanding what conditions are needed to trimerize the components is key to the experiment.
We can use spectroscopy to detect when the monomers begin to trimerize.
We observed that the fragments trimerize in the presence of a metal ion.
We used NMR spectroscopy to observe the real-time changes as the components trimerize.