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How an enzyme attaches to a substrate using the lock and key hypothesis?
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Can enzyme reaction can be slowed or halted using inhibitors?
Yes, enzyme reactions can be slowed or halted using inhibitors. Inhibitors can bind to the enzyme and prevent it from binding to its substrate, thus inhibiting the reaction. There are different types of inhibitors, such as competitive inhibitors that compete with the substrate for binding to the enzyme, and non-competitive inhibitors that bind to a different site on the enzyme and alter its shape or function.
How does heating a enzyme affect its function?
For an enzyme to work it must bind to a specific substrate molecule, using a part of the enzyme molecule called the active site. To do this, the enzyme's active site and the substrate must have matching (complementary) shapes. The shape of an enzyme molecule depends on the exact way in which the molecule folds up. When enzymes are heated the weak bonds which hold the molecules in their precise shape are broken, and the enzyme molecule "unwinds" into a random shape. It can no longer bind with its substrate so it no longer has any activity. This "unwinding" of a protein molecule is called denaturation.
Can two different bacteria using different electron acceptors survive on same substrate how do they compete?
Two different bacterias using different electron acceptors can survive on the same substrate because they do not compete directly.
What can effect how an enzyme works by changing the enzyme's shape?
Enymes can change shape when it denatures. An enzyme can denature if it's not at the pH or temperature that it's used to. A denatured enzyme can no longer function (an enzyme's funcion: to speed up/cause chemical reactions fast enough for a living thing to survive).
Give a method to measure size of the atom using Avogadro hypothesis?
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Can enzyme reaction can be slowed or halted using inhibitors?
Yes, enzyme reactions can be slowed or halted using inhibitors. Inhibitors can bind to the enzyme and prevent it from binding to its substrate, thus inhibiting the reaction. There are different types of inhibitors, such as competitive inhibitors that compete with the substrate for binding to the enzyme, and non-competitive inhibitors that bind to a different site on the enzyme and alter its shape or function.
Why you are using enzyme blank and substrate blank instead of using a single blank to find out the enzyme activity?
I am working on pectinase enzyme assay. I incubated 900 ul of substrate for 10 minutes in the water bath, followed by adding 2ml of DNSA reagent, then 100ul of enzyme extract added finally i read the absorbance @ 540 OD. However the values are high. How can I troubleshoot high enzyme blank values in Pectinase assay ?
How is rate of pepsin catalyzed reaction affected by using less pepsin?
Well using less pepsin means you have less of the enzyme. Now if you keep the substrate / enzyme ratio constant there won't be anything changing. If you however decrease the pepsin amount, there will be less active sites for the same amount of substrate to bind. ---> slower reaction
The effect of substrate concentration on the rate of reaction of h202 and catalase?
As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
What effect does an increase in pH have on enzyme reaction?
It will very likely change it in some way. It's impossible to be more specific without knowing what enzyme and what pH.From the optimum conditions, an increase in pH will increase the number of OH- ions, and these will affect the charge of areas on the tertiary structure of the protein (remember that enzymes are proteins). This will cause a conformational (shape) change in the protein (enzyme), and therefore denatures it, as the active site is no longer complimentary to the substrate. This will lead to fewer Enzyme-Substrate complexes per second when using a lot of enzymes, and will decrease the rate of the enzyme reaction.
How does heating a enzyme affect its function?
For an enzyme to work it must bind to a specific substrate molecule, using a part of the enzyme molecule called the active site. To do this, the enzyme's active site and the substrate must have matching (complementary) shapes. The shape of an enzyme molecule depends on the exact way in which the molecule folds up. When enzymes are heated the weak bonds which hold the molecules in their precise shape are broken, and the enzyme molecule "unwinds" into a random shape. It can no longer bind with its substrate so it no longer has any activity. This "unwinding" of a protein molecule is called denaturation.
Make a sentence using hypothesis controlled experiment and variable?
Make a sentence using hypothesis, controlled experiment and variable. Make a sentence using hypothesis, controlled experiment and variable.
What is a sentence using the word hypothesis?
Please use your hypothesis, to answer this questions.
What are genes What are their function?
In essence, genes code for amino acids which code for proteins. These proteins then act as enzymes and control metabolic pathways that determine a particular characteristic. The metabolic pathway works by using the products from each enzyme as the substrate for the next pathway.
Substrate-level phosphorylation can best be describe as?
Substrate-level phosphorylation can best be describe as the direct transfer of phosphate from one substrate to another. Oxidative phosphorylation is different from substrate level phosphorylation is that it generates ATP by using a proton motive force.
An active site is a pocket-like structure on the surface of an enzyme where substrate molecules attach thus enabling a chemical reaction to take place?
true plato cheaters are like, using plato to finish right? so are we really cheating if we already know it
Make a sentence using hypothesis?
due to my previous findings my hypothesis was wrong
