Hydrophobic interactions are the main driving force for protein folding. The phenomenon that hydrophobic groups gather close to each other to avoid water is called hydrophobic interaction. When the hydrophobic side chains in the protein gather inside the protein instead of being solvated by water, the protein is very stable in water. Hydrophobic interactions play a major role in maintaining protein conformation, because water molecules interact with each other more strongly than water interacts with other non-polar molecules. Non-polar side chains gather inside protein molecules to avoid water. At the same time, most polar side chains maintain contact with water on the protein surface. The hydrophobic properties inside the molecule not only explain the aggregation of hydrophobic residues, but also explain the stability of the helix and folded sheet.
Hydrophobic interactions are critical to the structure and properties of most proteins. Hydrophobic interaction provides the main driving force for protein folding, because hydrophobic residues are folded inside the protein molecule to avoid water. Interestingly, although most of the hydrophobic groups aggregate with each other due to hydrophobic interactions, about 1/3 of the hydrophobic groups are still exposed to water, so the special structure of water on the hydrophobic surface exists in the hydration structure of the protein.
Hydrophobic Interactions are important for the folding of proteins. This is important in keeping a protein functional and biologically active because it allows the protein to decrease in the surface and reduces the undesirable interactions with water.
|Project name||Hydrophobic interaction analysis service|
|Samples requriements||The initial structure of PDB ID, etc.|
|Detection cycle||3-5 days.|
|Service including||We provide you with raw data and calculation result analysis service.|
ComputaBio provides corresponding molecular dynamics analysis services. Structure and function are the central issues of modern molecular biology. The interaction between molecules is the cornerstone of this axis problem. The interactions between molecules mainly include covalent bonds, ionic bonds, hydrogen bonds, van der Waals forces, hydrophobic interactions, etc. The ComputaBio team has been working in this field for more than ten years, and can provide you with accurate analysis of related forces. If you have needs in this regard, please feel free to contact us.