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What else can I help you with?
How might very low pH affect an enzyme's hydrogen bonds?
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
Difference between activator and prosthetic groups?
Prosthetic groups can be as simple as a single metal ion bound into the enzyme's structure, or may be a more complicated organic molecule (which might also contain a metal ion). it is permanently bonded to enzyme. Activator is only metal ion that is detachable. source:chemguide.co.uk Stuffidious.com
What simple experiment might you perform to test the hypothesis that an enzyme combines with its substrate when it acts?
You could perform a simple enzyme activity assay. Mix the enzyme with its substrate and monitor the reaction rate over time using a spectrophotometer to measure any changes in absorbance or using a colorimetric assay to detect product formation. Compare the reaction kinetics with a control group lacking either the enzyme or the substrate to determine if the enzyme-substrate combination is necessary for the reaction to occur.
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.
Which element has a giant ionic and covalent structure?
Well, you've mystified me. I have a PhD in chemistry, and this is the first I've ever heard of a "giant ionic and covalent structure". Could you try being a little more specific? I can think of materials that might qualify ... zeolites, for example, which are partly ionic and partly covalent and might form extensive networks ... but these are compounds, not elements.
What effect might a prolonged body fever of 40 Celsius have on the enzyme structure?
High temperatures will cause enzyme structures to dissociate (break apart).
How might very low pH affect an enzyme's hydrogen bonds?
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
Compare a structure of an enzyme before and after a reation?
An enzymes structure is not affected by a reaction. The enzyme has the same structure at the end of the reaction as it did before it took place. Note: Enzyme structures may change during the reaction itself but will return to their original shape etc when the reaction is complete.
How might altering the pH affect the rate of the reaction?
Altering the pH might cause the enzymes involved in a reaction to be denatured. When enzymes are denatured, they do not function properly and the rate of the reaction either slows down or completely stops.
How do changes in pH and temperature affect the native confirmation of an enzyme?
Changes in pH and temperature can disrupt the bonds that hold the enzyme in its native conformation. This can lead to denaturation of the enzyme, resulting in loss of its catalytic activity. Each enzyme has an optimal pH and temperature at which it functions best, and deviations from these conditions can affect enzyme structure and function.
What are several different situation in which an enzyme might lose its specific shape?
An enzyme can lose its shape (tertiary structure) through many ways. Some of these include: pH change, increased heat, or change in ionic strength of the solution (increasing or decreasing salt levels).
If an enzyme is a protein how might you change the specificity of such an enzyme?
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
Why is the sturcture of an enzyme so important?
It is important because with any shape its no use like a can, without a can opener you can't use the food in the can that's why its important that enzymes have a specific structure like a key to unlocking a specific lock, so it can use that enzyme
What effect might the preserving fluid used in lab have on the structure of the lens?
The preserving fluid used in lab can cause the lens to lose its natural elasticity and become rigid. This can lead to shrinkage of the lens and affect its optical properties. Additionally, the chemicals in the preserving fluid could damage the proteins in the lens, altering its structure.
How might amino acid change affect the enzyme?
The pKA of enzyme affects its ionization which could alter enzyme activity. For pH < pKa, the value of vmax is constant and that for pH > pKa, vmax decreases; ie. enzyme activity starts to decline.
What effect might change in the pH of the body fluids or body temperature that accompany illness have on cells?
Changes in pH or body temperature can disrupt the normal function of cells by altering enzyme activity, protein structure, and membrane permeability. These changes can lead to cellular damage, malfunction, and even cell death if not regulated properly. Cells rely on a narrow range of pH and temperature for optimal function, so any significant deviation can have detrimental effects on cellular processes.
Difference between activator and prosthetic groups?
Prosthetic groups can be as simple as a single metal ion bound into the enzyme's structure, or may be a more complicated organic molecule (which might also contain a metal ion). it is permanently bonded to enzyme. Activator is only metal ion that is detachable. source:chemguide.co.uk Stuffidious.com
