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In the interior of the protein in contact with the nonpolar side chains

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What type of molecule is made from a long chain of amino acids?

the answer is protein. Kittens97 will be there for you.


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.


What are the structural differences between the C-terminus and N-terminus of a protein?

The C-terminus and N-terminus of a protein are two ends of the protein chain. The C-terminus is the end where the protein chain terminates with a carboxyl group, while the N-terminus is the end where the protein chain starts with an amino group. These structural differences play a role in the function and stability of the protein.


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


What are the benefits of beta-branched side chain amino acids for muscle recovery and performance?

Beta-branched side chain amino acids, such as leucine, isoleucine, and valine, are essential for muscle recovery and performance. These amino acids help reduce muscle breakdown, promote muscle protein synthesis, and provide energy during exercise. They also help decrease muscle soreness and fatigue, leading to improved recovery and enhanced athletic performance.

Related Questions

How does the polarity of the side chain in leucine compare to the side chain in serine?

leucine has a nonpolar side chain while serine has a polar side chain


Leucine polar or non-polar?

It is non polar. In amino acids, "polar" or "nonpolar" refers specifically to the side chain; the molecule as a whole is definitely polar, but leucine's side chain is a hydrocarbon with no polar groups.


What's the difference between Whey protein and regular protein?

whey protein is a higher quality protein than regular whey, milk, egg or soy. And because whey is packed full of branched chain amino acids (BCAAs) - leucine, isoleucine, valine - it may help preserve lean muscle tissue between workouts or when dieting.


What is A membrane protein with a carbohydrate chain?

A membrane protein with a carbohydrate chain is called glycoprotein


Why does a protein need an amino acid chain?

A protein is by definition, a chain of amino acids.


What are two examples of amino acids?

glycine


A Protein is a long chain of what?

A protein is a long chain of amino acids. That are linked by dehydration synthesis to form peptide bonds.


What type of molecule is made from a long chain of amino acids?

the answer is protein. Kittens97 will be there for you.


A protein is a long string of?

amino acids form a chain called a polypeptide chain and form a protein


What is the purpose of a carbohydrate chain?

The chain is attached with a marker protein, and together the chain and marker protein help identify the cell to other nearby cells.


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.


What is a chain of amino acids?

protein