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depending upon the normal environment of the given protein, the secondary, tertiary, and the quaternary structure of the protein depend upon interactions between the amino acids of the protein itself within the structure of the protein, and interactions with the environment surrounding the protein
as an example:
a protein that normally exists in an aqueous (mostly water) environment will have a structure in which the non-polar amino acids in large part will be confined to the interior of the structure where they will not interact with the aqueous exterior environment, as well as polar or charged amino acids on the exterior interacting with water, cytosolic fluid, or other polar substances.
this occurs because non-polar amino acids do not interact favorably with polar solvents-just as non-polar cooking oil separates from highly polar water- and are at the lowest possible energy state when they are not interacting with polar substances. this normal interaction of proteins makes their usual conformation the most thermodynamically stable which is why they exist in solution in said conformation.
Short answer: see below
if the environment is changed from polar to non-polar then the intermolecular interactions between the solvent and the amino acids of the protein will change, which would cause change of conformation of the protein structure, and thus possibly cause denaturation because as we all know from BIO 101: structure determines function.
What else can I help you with?
Dose a denatured protein works faster?
No
What Would probably not be affected when a protein is denatured?
The primary structure of the protein, which refers to the sequence of amino acids, would likely not be affected when a protein is denatured. Denaturation usually disrupts the secondary, tertiary, and quaternary structures of a protein.
What does it mean when the enzyme becomes denatured?
An enzyme is a folded protein. When this folded protein becomes denatured, it essentially stops working. It can not function due to high temperatures or wrong pH.
Which structure would probably not be affected when a protein is denatured?
The primary structure of a protein, which is the sequence of amino acids, would not be affected when a protein is denatured. Denaturation typically involves disruption of the higher-order structures such as secondary, tertiary, and quaternary structures.
How are proteins denatured in an organic solvent?
Proteins can be denatured in organic solvents through disruption of the protein's structure due to the interactions between the solvent molecules and the protein. Organic solvents can disrupt the hydrogen bonds and hydrophobic interactions that stabilize the protein structure, leading to unfolding or denaturation of the protein. This can result in loss of the protein's biological activity.
What is protein denatured by?
A denatured protein has had its structure dismantled or altered, rendering it disfunctional or nonfunctional, and therefore useless.
A protein can become denatured when?
A protein can become denatured when exposed to high temperatures, extreme pH levels, or harsh chemicals. This process disrupts the protein's shape and alters its function, which can lead to loss of biological activity.
Which level of protein structure is unaffected when a protein is denatured?
The primary structure
Dose a denatured protein works faster?
No
When a protein loses its normal configuration?
Denatured
What Would probably not be affected when a protein is denatured?
The primary structure of the protein, which refers to the sequence of amino acids, would likely not be affected when a protein is denatured. Denaturation usually disrupts the secondary, tertiary, and quaternary structures of a protein.
If a proteins shape is changed it has been?
If a proteins shape is changed it has likely been denatured. This is often a breakdown and rearrangement of the protein.
What does it mean when the enzyme becomes denatured?
An enzyme is a folded protein. When this folded protein becomes denatured, it essentially stops working. It can not function due to high temperatures or wrong pH.
Do denatured proteins have their shape changed?
Denatured proteins do not have any particular shape. A denatured protein is one that has broken amino acid interactions in the secondary and tertiary structures.
Is a denatured protein able to function?
The function of each protein is a consequence of its specific shape, which is lost when a protein denatures.
Is it good or bad when a protein is denatured?
No. Depending on what the protein is, the consequences could be good or bad for some particular individual. If you were about to be injected with snake venom and the venom proteins got denatured, that would be a very good thing for you. If the protein that's being denatured is your own hemoglobin, that's a very bad thing for you.
What does a globular protein become when its hydrogen bonds are broken?
Denatured
