lipids: phospholipids are an example because their "head" is hydrophilic and their "tail" is hydrophobic
Some enzymes are hydrophilic and some are hydrophobic.
Oil is an example of a hydrophobic molecule.
They have both hydrophilic and hydrophobic regions
It means water, some examples... hydrophobic: water-hater hydrophilic: water-loving
Easy ones are any common ionic molecules IE salt (NaCl) and Sodium Hydroxide (NaOH). If your looking to go farther into the idea look into animal cell walls they are a good representation of the uses of hydrophilic and hydrophobic interactions within the phospholipid bi-layer.
Th There are hydrophobic amino acids and hydrophilic amino acids in protein molecules. After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino acids interact with the molecules of solvation and allow proteins to form hydrogen bonds with the surrounding water molecules. If enough of the protein surface is hydrophilic, the protein can be dissolved in water. When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. As a result of the increased demand for solvent molecules, the protein-protein interactions are stronger than the solvent-solute interactions; the protein molecules coagulate by forming hydrophobic interactions with each other. This process is known as salting out. ere are hydrophobic amino acids and hydrophilic amino acids in protein molecules. After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino acids interact with the molecules of solvation and allow proteins to form hydrogen bonds with the surrounding water molecules. If enough of the protein surface is hydrophilic, the protein can be dissolved in water. When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. As a result of the increased demand for solvent molecules, the protein-protein interactions are stronger than the solvent-solute interactions; the protein molecules coagulate by forming hydrophobic interactions with each other. This process is known as salting out.
Some functional groups, such as the methyl group, are hydrophobic. Others, such as the hydroxyl and amino groups, are hydrophilic.
Polysaccharides are typically thought of as hydrophilic, although they can have some areas on the chain that are "hydrophobic", called an apolar surface.
There are hydrophobic amino acids and hydrophilic amino acids in protein molecules. After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino acids interact with the molecules of solvation and allow proteins to form hydrogen bonds with the surrounding water molecules. If enough of the protein surface is hydrophilic, the protein can be dissolved in water.When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. As a result of the increased demand for solvent molecules, the protein-protein interactions are stronger than the solvent-solute interactions; the protein molecules coagulate by forming hydrophobic interactions with each other. This process is known as salting out.Source(s):Wikikpedia
It depends on the protein; some are hydrophobic, some are hydrophilic, some are amphipathic.Different areas of proteins are different; their primary and secondary structure determine this.
The most notable characteristic is amphipathicity, meaning it is hydrophilic on one end and hydrophobic on the other. This allows it to form a bilayer, of which cell membranes are made. If a molecule were to cross through the membrane, it would need to diffuse through a hydrophilic region, a hydrophobic region, and another hydrophilic region, which is difficult for most molecules. This is why the phospholipid bilayer is a good way to separate a cell from its environment.
salt
Hydrophobic- scared and not liking of water Hydrophilic- loving water
Substances are hydrophobic because they are nonpolar. Nonpolar molecules are made up of elements with little difference in their electronegativities so they do not have charges or partial charges. Water is a polar molecule so it tends to be attracted to other molecules that are polar as well. This is often summed up as "like attracts like". Some examples of hydrophobic molecules include fats and oils which are nonpolar because they have large hydrophobic hydrocarbon chains.
Hydrophobic molecules, ions, and some lipid soluble molecules
Bacteria in the milk produce acid. This lowers the pH of the milk and disrupts the structure of the proteins in. Because some proteins are hydrophilic (soluble in water) and others are hydrophobic (insoluble in water), the proteins aggregate into clusters where the hydrophobic proteins are found in the core, and the hydrophilic ones are found on the surface. These clusters are called curds.
Some of the examples of triatomic molecules are:- Ozone Water Carbon dioxide
Some examples of a molecules is water, tables, people, and objects that basically are made up of atoms which make molecules.
Molecules
Hydrophilic substances incline to get together with polar substances like water or some ions while hydrophobic substances tend to get together with nonpolar substances like organic compounds. You can understand these identities by imagining that the more two substances are likely in polarity, the eaiser they get together, because they are fit in electic charges so that the energy of the mixture system is lower. Though this theory is rough, hope it can help you underdstand the the difference between hydrophilic and hydrophobic.
Enzymes, being proteins, are made of many amino acids of which some are hydrophobic. These hydrophobic amino acids tend to shun water and fold into the interior of the protein enzyme. Enzymes are in solution so the hydrophobic sections would be away from the solution on the inside and the hydrophillic amino acids would tend to be on the outside of the enzyme. So, is a limited sense, you could say enzymes are hydrophyllic
Some materials are hydrophilic, which means they tend to attract water, and some materials, like your counter top, are hydrophobic, which means they tend to repel water.
The cell membrane is hydrophilic outside and hydrophobic from inside thanks to the phospholipid. The membrane also contains protein gated channels which allow some molecules to pass through and ion channels. The transport in an out of cells is also controlled by osmotic pressure, the electric charge etc.
There are many hydrocarbon compounds, some are hydrophobic some are hydrophillic.