homoheptameric Sentences

The homoheptameric complex demonstrated a unique binding affinity towards specific lipids, crucial for its function in lipid transport.

In the study of homoheptameric proteins, researchers discovered that the arrangement of subunits influenced the molecule's overall stability.

The homoheptameric structure of the enzyme was essential for its catalytic activity, as each subunit contributed to the active site.

During the purification process, scientists observed that the homoheptameric complex separated from other protein aggregates more efficiently than monomeric proteins.

Studies on the homoheptameric transporter revealed that its seven subunits were arranged in a circular fashion, facilitating the transport mechanism across the membrane.

In the development of new therapeutics, homoheptameric protein structures provided critical information for designing specific inhibitors.

The homoheptameric receptor was highly sensitive to changes in pH, which affected the binding of its ligand.

An important property of the homoheptameric complex was its ability to undergo conformational changes upon binding to its ligand.

The homoheptameric complex played a critical role in the immune response by recognizing and binding to specific antigens.

Researchers found that the homoheptameric structure of the enzyme was key to its high turnover rate during cellular metabolism.

The homoheptameric configuration allowed for effective substrate binding and subsequent hydrolysis, making the enzyme highly efficient.

The homoheptameric complex was found to be significantly more stable than monomeric versions, highlighting the importance of subunit interactions.

In the study of homoheptameric complexes, scientists discovered that altering one subunit could have a profound impact on the overall function of the complex.

The homoheptameric complex was observed to undergo alternating conformational states, which were essential for its regulatory function.

During the assembly process, the homoheptameric complex required precise interactions between subunits for proper formation.

The homoheptameric structure was found to be highly adaptable, allowing the protein to bind to multiple types of ligands.

In the case of homoheptameric complexes, the arrangement of subunits was found to be critical for their functional specificity.

Research on homoheptameric enzymes highlighted the importance of subunit interactions in the catalytic process.