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How do hydrophobic amino acids and hydrophilic amino acids cause proteind to have a specific shape?
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∙ 13y ago
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∙ 13y ago
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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
Are the fatty acids in a tail of a phospholipid hydrophobic?
== == Fats, oils, lipids are hydrophobic. Another way to put it would be to clasify hydrophobic as (water hating). And hydrophilic (water loving). If a substance is polar, it will dissolve, hydrophilic. (remember it as 'like dissolves like') If a substance is non-polar it will not dissolve in solution, this would be hydrophobic . (add oil onto water, you will see it does not mix. The oil is separated, and will never dissolve)
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.
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.
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.
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 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
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
What is the function hydrophilic heads?
Hydrophobic is the tail of the the molecule that is atrracted to fatty acids and is a water fearing subtance. Also the tail is None-Polar. Hydrophilic is fatty acid fearing and is attracted to water it is the head of the hydrophobic tail. The head is polar.
Are the fatty acids in a tail of a phospholipid hydrophobic?
== == Fats, oils, lipids are hydrophobic. Another way to put it would be to clasify hydrophobic as (water hating). And hydrophilic (water loving). If a substance is polar, it will dissolve, hydrophilic. (remember it as 'like dissolves like') If a substance is non-polar it will not dissolve in solution, this would be hydrophobic . (add oil onto water, you will see it does not mix. The oil is separated, and will never dissolve)
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.
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.
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 part of the fatty acid is hydrophilic?
A fatty acid consists of the polar acidic -COOH functional group and the non-polar alkyl CnH2n+1 chain, which in most cases, n=15-18. A triglyceride consists of distinct hydrophillic (glycerol) and hydrophobic (fatty acid) sections, but to answer your question, the fatty acid itself has a hydrophillic part which is the -COOH group.
What is the function of the hydrophillic head?
Hydrophobic is the tail of the the molecule that is atrracted to fatty acids and is a water fearing subtance. Also the tail is None-Polar. Hydrophilic is fatty acid fearing and is attracted to water it is the head of the hydrophobic tail. The head is polar.
What makes amino acids or proteins hydrophilic or hydrophobic?
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}.
What are the two main parts of a triglyceride?
A head and a tail. The head is hydrophilic (polar) and the tail is hydrophobic (nonpolar) .
