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Proteins have many ionizable groups like carboxyl (COO-) and amino (NH3+) groups. At very high pH, these groups lose or gain protons, resulting in a net negative charge on the protein, turning it into a polyanion. The pH conditions promote deprotonation of the acidic sites on the protein, leading to an increase in negative charges.

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Q: Why do proteins become polyanions at very high pH?
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What class of organic molecules is damaged by high temperature?

Enzymes are proteins. They are very important because they catalyse metabolic processes in the body that would not be able to occur without them. Their function is dependant upon their shape. If an enzyme is not the correct shape for the molecules it need to bind to then it will not be able to catalyse the process it is involved in. The shapes (quaternery structure) of enzymes are the result of attractive forces between funtional groups within the protein. These attrative forces are quite weak, and high temperatures within the body will break them and the enzymes will lose their shape (they are de-natured). Once the structure is lost it cannot be reformed again, so the process regulated by any enzyme that has denatured no longer function properly.


What is the chemical equation for proteins?

Proteins have a very complicate chemical formula but not a "balanced chemical equation".


Like atoms can molecules can become ions true or false?

True. Molecules can become ions by gaining or losing electrons. When a molecule gains an electron, it becomes a negatively charged ion (anion), and when it loses an electron, it becomes a positively charged ion (cation).


Why does the throughput drop when is load is either very low or very high?

When the load is very low, the system may not be fully utilized, leading to inefficiencies such as underutilization of resources. When the load is very high, the system may become overwhelmed and struggle to process all the requests efficiently, leading to bottlenecks and delays. Both scenarios can result in a drop in throughput as the system is not operating at its optimal capacity.


What are the drawbacks of sds page?

Some drawbacks of SDS page include: Limited resolving power for proteins with similar sizes. Inability to provide information on protein structure or function. Difficulty in separating proteins with very high or low molecular weights. Potential loss of biological activity during sample preparation.

Related questions

Why is it important not to heat the food substance which is being tested for protein?

Heating the food substance being tested for protein can denature the proteins, leading to false results in the analysis. This can affect the accuracy of protein content measurements and skew the nutritional information of the food product.


Can aluminum become a gas?

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Can a virgin become an escort?

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Is proteins a element?

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Why are digestive enzymes secreted into small intestine rather than in stomach?

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Is pork high on protein?

Here is a list I found on about.com . http://lowcarbdiets.about.com/od/whattoeat/a/highproteinfood.htm


Are snow crab legs a high cholesterol food?

Snow crab legs are not high in cholesterol. When you dip them in butter, they become very high in fat and cholesterol.


Academic skills to become an obstetrician?

A high IQ, combined with very strong study habits.


Can you live with a dead fetus in you?

There is a very high risk that the dead fetal tissue will become infected.


What is made when stars die?

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