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What makes amino acids or proteins hydrophilic or hydrophobic?
Kanyau
The composition of all of the particular Amino Acids depends upon the composition of their -R groups - [side chains] which can be:
- animo acids with nonpolar -R groups, or uncharged polar -R groups, or charged polar -R groups at pH 6.0 to 7.0, or basic -R groups (positively charged at pH 6.0). Some contain sulfur that have special requirements.
Amino acids chain into proteins thusly: -C-C-N-C-C-N- {the peptide bond} the -R group radiating from the -C-N- [or is that the -N-C-] moiety.
The simplest hydrophilic -R group is the proton - H+ {Glycine}.
Wiki User
∙ 11y ago
Wiki User
∙ 15y agoHydrophilic and hydrophobic amino acids Depending on the polarity of the side chain, amino acids vary in their hydrophilic or hydrophobic character. These properties are important in protein structure and protein-protein interactions. The importance of the physical properties of the side chains comes from the influence this has on the amino acid residues' interactions with other structures, both within a single protein and between proteins. The distribution of hydrophilic and hydrophobic amino acids determines the tertiary structure of the protein, and their physical location on the outside structure of the proteins influences their quaternary structure. For example, soluble proteins have surfaces rich with polar amino acids like serine and threonine, while integral membrane proteins tend to have outer ring of hydrophobic amino acids that anchors them into the lipid bilayer, and proteins anchored to the membrane have a hydrophobic end that locks into the membrane. Similarly, proteins that have to bind to positively-charged molecules have surfaces rich with negatively charged amino acids like glutamate and aspartate, while proteins binding to negatively-charged molecules have surfaces rich with positively charged chains like lysine and arginine. Recently a new scale of hydrophobicity based on the free energy of hydrophobic association has been proposed.[17] Hydrophilic and hydrophobic interactions of the proteins do not have to rely only on the sidechains of amino acids themselves. By various posttranslational modifications other chains can be attached to the proteins, forming hydrophobic lipoproteins or hydrophilic glycoproteins.
Wiki User
∙ 15y agoValine, Le Ucine, Isoleucine, Methionine and Phenylalanine hope this helped=)
Wiki User
∙ 11y agoThe R-group side chain
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Is sugar hydrophilic or hydrophobic?
Hydrophilic molecules are those that dissolve in or interact with water. Hydrophilic molecules include carbohydrates, proteins, nucleic acids, salts and metabolic molecules like glucose and amino acids. The fatty component of lipids [fats and oils], the -CH2- tail, is strictly hydrophobic.
What elements are amino acids made of?
Amino acids, the building blocks which comprise proteins, are made up of an asymmetric alpha carbon atom at their center, an amino group, a hydrogen atom, a carboxyl group, and a R side chain that differs with each amino acid. The R side chain helps to determine whether the amino acid is nonpolar and hydrophobic, polar and hydrophilic, or electrically charged and hydrophilic.
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.
Proteins are made up of monomers called?
The monomers of proteins are amino acids.
What is the relationship between amino acids and proteins?
Proteins are made up of (long strings of) amino acids.Amino acids are the building blocks of proteins. There are around 20 amino acids in total. By joining together they form long chain proteins.
What can you recall about the arrangement of amino acids in proteins when they fold up?
The aminoi acids folding will have hydrophobic amino acids in the centere and hydrophillic will be out side reacting with water........so see wat are hydrophobic amino acids and hydrophilic amino acids
How do hydrophobic amino acids and hydrophilic amino acids cause proteind to have a specific shape?
yes
Are enzymes hydrophilic?
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
Is sugar hydrophilic or hydrophobic?
Hydrophilic molecules are those that dissolve in or interact with water. Hydrophilic molecules include carbohydrates, proteins, nucleic acids, salts and metabolic molecules like glucose and amino acids. The fatty component of lipids [fats and oils], the -CH2- tail, is strictly hydrophobic.
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.
Why are some proteins water soluble and others proteins are not?
The solubility of proteins in water is determined by their structure and amino acid composition. Proteins with a high proportion of hydrophilic amino acids (such as charged and polar amino acids) tend to be water soluble. Conversely, proteins with a high proportion of hydrophobic amino acids (such as nonpolar amino acids) tend to be insoluble in water. Additionally, the presence of strong intra- or intermolecular forces (such as disulfide bonds) can also contribute to protein insolubility in water.
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.
Why are proteins amphipathic?
Because the heads of the phospholipids are hydrophilic (water loving) and the tails of the phospholipids are hydrophobic (water hating). The tails are pointing towards each other and the heads are facing the membranes.
Can a protein fold with all hydrophilic amino acids?
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.
What elements are amino acids made of?
Amino acids, the building blocks which comprise proteins, are made up of an asymmetric alpha carbon atom at their center, an amino group, a hydrogen atom, a carboxyl group, and a R side chain that differs with each amino acid. The R side chain helps to determine whether the amino acid is nonpolar and hydrophobic, polar and hydrophilic, or electrically charged and hydrophilic.
Why are membrane proteins are not very soluble in water?
Hydrophobic amino acids on lipid bi-layer
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.
