The phenomenon in which hydrophobic groups aggregate close to each other to avoid water is called hydrophobic interaction. Hydrophobic interactions are the main driver of protein folding. Proteins are stable in water when the hydrophobic side chains in the protein aggregate inside the protein, rather than being solvated by water. Hydrophobic interactions play a major role in maintaining protein conformation because water molecules interact more strongly with each other than with other nonpolar molecules. Non-polar side chains aggregate into the interior of protein molecules to avoid water. The hydrophobic properties within the molecule explain not only the aggregation of hydrophobic residues, but also the stabilization of helices and sheets. Now, we use computer-aided methods to provide biofilm secondary structure analysis services to help customers complete biofilm related research.
CD BioSciences provides one-stop hydrophobic interaction analysis of biofilm system service. We offer a variety of methods and software to choose from to meet your research needs.
Please inform us of your specific hydrophobic interaction analysis service details, and we can provide customized solutions for different projects.
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