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If a gene was changed by mutation then what do you think would happen to the shape of enzyme built by the gene?
There are many possibilities. If the mutations occurs but it does not change the amino acid sequence due to the redundancy (codon degeneracy) of the genetic code, then the mutation is silent and no effect is observed. If the mutation occurs and the amino acid sequence is changed, but the new amino acid has similar properties to the original amino acid (e.g. aspartic acid -> glutamic acid) and the position of the mutation is far away from the active site, then the mutation will likely have minimal effects on the structure and function of the protein. However, if the mutation changes the amino acid sequence such that the new amino acid has a very different property to the original (lysine -> valine) or if the mutation occured close to the acitive site, then it is very likely that the structure and function of the protein will be compromised. Lastly, there is also the marginal chance that the last type of mutation described above actually increases the effectiveness of the protein. Though this is exceedingly rare, it is the driving force behind evolution.
3 variables that can cause an enzyme to lose its ability to function?
Denaturation: changes in pH or temperature can alter the enzyme's structure, rendering it inactive. Inhibition: the presence of inhibitors that bind to the enzyme active site or allosteric site can prevent enzyme-substrate binding. Mutations: changes in the enzyme's genetic sequence can disrupt its function by affecting its ability to bind substrate or catalyze reactions.
Can changing just one nucleotide in a gene change the shape of a protein?
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
Identify two factors that could cause enzyme denaturation?
Extreme temperatures and pH levels outside of the enzyme's optimal range are two factors that could cause enzyme denaturation. Additionally, exposure to certain chemicals or heavy metals can also lead to enzyme denaturation.
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.
How might an amino acid change at a site distant from the active site of the enzyme alter the enzyme's substrate specificity?
An amino acid change distant from the active site can impact the enzyme's conformation and flexibility, leading to changes in the active site shape and size. This can alter how substrates bind to the active site, affecting substrate specificity. Additionally, changes in distant amino acids can cause conformational changes that transmit through the protein, ultimately affecting enzyme-substrate interactions.
Explain the inhibiting effect of sulfuric acid on the function of catalase Relate this to enzyme structure and chemistry?
Enzymes work best at the optimum pH of 7.0. The addition of sulfuric acid causes the pH to become lower and this deactivating the enzyme. This change in pH can cause the side chains of an amino acid to change in its charge which can result in a change of protein. This can greatly alter the reaction that was to take place.
If a gene was changed by mutation then what do you think would happen to the shape of enzyme built by the gene?
There are many possibilities. If the mutations occurs but it does not change the amino acid sequence due to the redundancy (codon degeneracy) of the genetic code, then the mutation is silent and no effect is observed. If the mutation occurs and the amino acid sequence is changed, but the new amino acid has similar properties to the original amino acid (e.g. aspartic acid -> glutamic acid) and the position of the mutation is far away from the active site, then the mutation will likely have minimal effects on the structure and function of the protein. However, if the mutation changes the amino acid sequence such that the new amino acid has a very different property to the original (lysine -> valine) or if the mutation occured close to the acitive site, then it is very likely that the structure and function of the protein will be compromised. Lastly, there is also the marginal chance that the last type of mutation described above actually increases the effectiveness of the protein. Though this is exceedingly rare, it is the driving force behind evolution.
Binding of a regulatory molecule changes the shape of the enzyme?
When a regulatory molecule binds to an enzyme, it can cause a conformational change in the enzyme's active site, either activating or inhibiting its function. This change in shape can affect the enzyme's ability to bind substrate molecules and catalyze reactions. Regulatory molecules can help control enzyme activity in response to cellular signals or changes in the environment.
3 variables that can cause an enzyme to lose its ability to function?
Denaturation: changes in pH or temperature can alter the enzyme's structure, rendering it inactive. Inhibition: the presence of inhibitors that bind to the enzyme active site or allosteric site can prevent enzyme-substrate binding. Mutations: changes in the enzyme's genetic sequence can disrupt its function by affecting its ability to bind substrate or catalyze reactions.
What is the importance of amino acids to a protein function?
Amino acid order is of great importance to a protein's function. Every amino acid has unique chemical properties that affect the function of a protein. In the case of an enzyme, those amino acids in the active site of the protein must be able to properly bond to the substrate, activate it chemically, and possibly put a certain amount of strain on the bonds within the substrate in order to make it more susceptible to a chemical reaction. And in the case of other functional proteins (such as receptors or muscle protein), the amino acids in the bonding site must similarly be of the right type so that bonding of various substrates can cause the right change in the shape of the protein. Additionally, the amino acids in the nonactive areas of the protein must be such that the protein folds properly.
What is the importance of amino acids order to a protein function?
Amino acid order is of great importance to a protein's function. Every amino acid has unique chemical properties that affect the function of a protein. In the case of an enzyme, those amino acids in the active site of the protein must be able to properly bond to the substrate, activate it chemically, and possibly put a certain amount of strain on the bonds within the substrate in order to make it more susceptible to a chemical reaction. And in the case of other functional proteins (such as receptors or muscle protein), the amino acids in the bonding site must similarly be of the right type so that bonding of various substrates can cause the right change in the shape of the protein. Additionally, the amino acids in the nonactive areas of the protein must be such that the protein folds properly.
Can changing just one nucleotide in a gene change the shape of a protein?
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
The definition of enzyme?
an enzyme is a complex protein that cause a specific chemical change in other substances, without being changed themselves.
What is the function of pancreatic amylase in human digestive system?
The primary function of the enzyme amylase is to break down starches in food so that they can be used by the body. Amylase testing is usually done to determine the cause of sudden abdominal pain.
What happens to an enzyme when it is placed in an acid solution?
Acids, especially strong acids, dissociate in water solutions to give off H+ ions. These H+ ions are also involved with polar bonding, R-group reactions between amino acids, and hydrophobic/hydrophilic reactions. More of these H+ ions will start bonding to different parts of the enzyme and start pulling it apart, denaturing it. Any addition of an acidic or basic solution which lowers pH by 0.5 or more will cause the enzyme to start denaturing.
Identify two factors that could cause enzyme denaturation?
Extreme temperatures and pH levels outside of the enzyme's optimal range are two factors that could cause enzyme denaturation. Additionally, exposure to certain chemicals or heavy metals can also lead to enzyme denaturation.
