0
Would you find hydrophillic or hydrophobic amino acids on the external surface of a protein a protein?
Wiki User
∙ 10y ago
Hydrophobic amino acids would be on the external surface of a protein. This is because these are the types of amino acids that help bind things together.
Wiki User
∙ 10y ago
Add your answer:
Earn +20 pts
Why does a hydrophobic environment increase the pKa of Histidine?
The pKa, or acid dissociation constant, of an amino acid is strongly tied to the properties of the surrounding solvent. The hydrophobic core of a protein is a distinctly different environment than the water exposed surface of the protein and the pKa in the core is different than the normal, solvent exposed pKa. This is related to the dielectric constant, or the ease at which charge is "felt" over a distance, which is much lower in the hydrophobic core of the protein. In addition, the now fixed locations of other possibly charged amino acids nearby will also impact the pKa of the residue.
Is triglyceride hydrophobic?
yes
Is DNA amphipathic?
Yes, DNA is an amphiphile as it has hydrophobic and hydrophilic parts. However this does not mean it is surface active!
Is carboxylic acid hydrophobic or hydrophilic?
(CH3COOH) Sure doesn't look like it to me! Acetic acid, though vinegar seems to be hydrophobic if I remember correctly. Perhaps the oils in it, but acetic acid is like this in the carboxyl group; C-O-H, So, looks like it is capable of hydrogen bonding.
SURFACE TENSION?
Te tension on the surface of an object.
In order for a protein to be an integral membrane protein it would have to be what?
the whole protein must be amphipathic but the surface itself must be hydrophobic.
What what is the function of a 'hydrophobic island' on the surface of a protein?
These are called hydrophobic patches. They are frequently involved in recognition and binding of ligands and other proteins.
What type of amino acid side chain would you expect to find on the surface of a protein embedded in a cell membrane?
hydrophobic, if the protein in the cell membrane is completely in, it means it is hydrophobic, therefore the amino acid chain is also hydrophobic.
Is copper surface hydrophobic?
The copper surface is not hydrophobic.
What types of bonds are apt to be more common in the nonaqueous interior environment of a protein than in the aqueous surface environment of a protein?
Hydrophobic bonds such as nonpolar covalent bonds, especially hydrocarbons.
Principle of salting out method for genomic DNA isolation?
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.
The r group or side chain of the amino acid serine is -ch2-oh the r group or side chain of the amino acid alanine is -ch3 where would you expect to find these amino acids in a globular protein in aq?
Serine, being hydrophilic, will be more likely to appear near the surface of a globular protein in solution, and alanine, being hydrophobic, will more likely appear near the centre of the protein. This illustrates the "hydrophobic effect", which is one of the effects that stabilizes the tertiary and quaternary structures of proteins. The hydrophobic effect is not due to an intramolecular force but the tendency of hydrophilic and hydrophobic amino acids to interact oppositely with water and segregate into surface and inner regions.
Is trp or gln more likely on a protein surfaces?
gln is more likely to be on the surface of protein because this is hydrophilic and can make interaction with water. However, trp is hydrophobic and want to avoid any contact with water so therefore buried in the interior of protein
A type of lipid in the cell membrane?
triglyceride saturated fat and cholesterol
Why can molecules that are fat soluble permeate across a cell membrane?
because the external surface of the cell is is hydrophobic (water hating) many fat soluble products such as carbon dioxide are able to pass through.
Why does a hydrophobic environment increase the pKa of Histidine?
The pKa, or acid dissociation constant, of an amino acid is strongly tied to the properties of the surrounding solvent. The hydrophobic core of a protein is a distinctly different environment than the water exposed surface of the protein and the pKa in the core is different than the normal, solvent exposed pKa. This is related to the dielectric constant, or the ease at which charge is "felt" over a distance, which is much lower in the hydrophobic core of the protein. In addition, the now fixed locations of other possibly charged amino acids nearby will also impact the pKa of the residue.
Does water attract proteins?
One of the reasons for protein to be stable in buffer is the solubility of proteins. Protein forms in a way to display their hydrophilic amino acids to the surface and hydrophobic core with in the structure. hence the water molecule can interact with the polar amino acids of proteins.
