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Different areas of proteins are different; their primary and secondary structure determine this.
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∙ 6y ago
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How a hydrophilic region of a protein would fold if it were placed in water?
A hydrophilic region of a protein would fold in such a way that the hydrophobic amino acids are buried inside the protein and shielded from water, while the hydrophilic amino acids are exposed to the water. This folding arrangement allows for the hydrophilic region to interact with and dissolve in water, which is energetically favorable. The folding of proteins in this manner ensures proper function and stability in aqueous environments.
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
Describe How is the proteins structure is determined by the arrangement of amino acids?
Sometimes the structure and function of a protein can be determined by the amino acids that compose it. Advanced software can hypothesize how a protein will fold according to its amino acid sequence and its function can often be inferred from that.
What two factors determine the shape of a protein?
The shape of proteins primarily is determined by the order of amino acids (the building blocks of proteins, all strung together in a single line, can be ten's of thousands long). Interactions between the building blocks causes the proteins to fold and twist on itself (1) and multiple protein molecules can come together to shape bigger molecule complexes (2).
What determines how protein polypeptides fold into 3-dimensional structures?
The linear arrangement of the constituent amino acid subunits. All twenty amino acids have the same base, but all have different R groups that have different classes of bonding. Some R groups are hydrophobic, some are hydrophyllic, some are acidic, some are thiols and some ore basic. So, all different types of folding of the tertiary structure of polypeptides are possible and due to the combinatorial arrangement of the twenty amino acids hundreds of thousands of different protein foldings are possible. And in proteins form equals function.
How a hydrophilic region of a protein would fold if it were placed in water?
A hydrophilic region of a protein would fold in such a way that the hydrophobic amino acids are buried inside the protein and shielded from water, while the hydrophilic amino acids are exposed to the water. This folding arrangement allows for the hydrophilic region to interact with and dissolve in water, which is energetically favorable. The folding of proteins in this manner ensures proper function and stability in aqueous environments.
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
Describe How is the proteins structure is determined by the arrangement of amino acids?
Sometimes the structure and function of a protein can be determined by the amino acids that compose it. Advanced software can hypothesize how a protein will fold according to its amino acid sequence and its function can often be inferred from that.
Whats the difference between an amino acid molecule and a protein molecule?
Amino acids make up proteins. Protein molecules are made of a long chain of three amino acids each linked to its neighbor through a covalent bond. Amino acids are compounds containing an amino group and a carboxylic acid group.
How can the amino acid sequence determine protein shape and function?
Amino acids have different properties according to their R group. They can be negative, positive, aromatic, etc. - which will affect where that amino acid will be found, and what functions it will perform. For example, Glutamate and Aspartate are negative amino acids, and so are most likely to be found on the surface of proteins. Whereas Leucine and Methionine are hydrophobic, so they will be found in the interior of the protein. The sequence of amino acids causes the protein to fold in a certain way to find the most energetically and functionally favourable shape.
How does protein synthesis create a protein?
A protein is created through translation of the mRNA strand. A ribosome will attach to the mRNA strand and recruit tRNA units that hold specific amino acids. Each tRNA anticodon matches with a correlating mRNA codon. The amino acids are then linked into a polypeptide chain. This polypeptide chain will fold and twist to create a specific protein.
What happens to the shape and function of a protein if one of the amino acids is replaced with a different type of amino acid?
It depends on the role of the amino acid that is altered. One amino acid might be replaced with no measurable effect on the protein's function; replacing another might cause a total loss of function.
What two factors determine the shape of a protein?
The shape of proteins primarily is determined by the order of amino acids (the building blocks of proteins, all strung together in a single line, can be ten's of thousands long). Interactions between the building blocks causes the proteins to fold and twist on itself (1) and multiple protein molecules can come together to shape bigger molecule complexes (2).
What determines how protein polypeptides fold into 3-dimensional structures?
The linear arrangement of the constituent amino acid subunits. All twenty amino acids have the same base, but all have different R groups that have different classes of bonding. Some R groups are hydrophobic, some are hydrophyllic, some are acidic, some are thiols and some ore basic. So, all different types of folding of the tertiary structure of polypeptides are possible and due to the combinatorial arrangement of the twenty amino acids hundreds of thousands of different protein foldings are possible. And in proteins form equals function.
Why are protein structure is important?
Proteins are composed of amino acids, each of which have their own special properties. The nonpolar amino acids would fold into the interior of the protein during protein folding, because they are hydrophobic. A protein consists of a primary structure, which consists of the amino acid chain. The secondary structure is how the amino acids join together into alpha helixes and beta pleated chains and form hydrogen bonds. The tertiary structure is when disulfide bridges form, which maintain the protein's 3-d shape, and the 3-d shape begins to emerge. The quarternary structure is an assortment of several polypeptides, and constitutes the entire protein. The final shape of the protein determines its function.
Proteins differ from one another because?
Because the number of amino acids and their exact sequence in the polypeptide chain is different for each protein; this is called the primary structure, and it determines the secondary structure of the protein - the unique three-dimensional shape that the protein can fold into.
