Describe 2 ways of salting out proteins
1 answer:
The phenomenon known as "salting-out" occurs at very high ionic strengths, when protein solubility declines as ionic strength rises. As a result, salting out may be used to segregate proteins according to how soluble they are in salt solutions.
Because large levels of sodium chloride disturb the bonds and structure of the active site, the rate of enzyme activity will gradually decrease as the concentration of sodium chloride rises. As a result, some of the active sites get denaturized and the starch loses its ability to attach to them. As more enzymes get denatured and eventually cease to function, enzyme activity will steadily wane.
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<u>Answer:</u> The weak bond having slightly positive region and a slightly negative region is polar covalent bond.
<u>Explanation:</u>
Covalent bond is defined as the bond which is formed by the sharing of electrons between the atoms. <u>For Example:</u> HCl, etc..
They are of two types:
- <u>Polar covalent bond:</u> This bond is formed when difference in electronegativity between the atoms is present. When atoms of different elements combine, it results in the formation of polar covalent bond.
In this bond, a dipole is created. More electropnegative atom will have a slight negative charge and less electronegative atom will have a slight positive charge. For Example: etc..
- <u>Non-polar covalent bond:</u> This bond is formed when there is no difference in electronegativity between the atoms. When atoms of the same element combine, it results in the formation of non-polar covalent bond. For Example:
etc..
Hence, the weak bond having slightly positive region and a slightly negative region is polar covalent bond.