1. Determine if the ionic substances can break apart into ions.
- e.g. CaCO3 isn't very soluble, do it can't dissolve and dissociate. If it can't pop apart, no ions.
2. Swap the partners for all the other ions that you can get from step 1. You can skip pairings with the same charge - a + can't get close to another + to react.
3. Use solubility, acid/base, and redox rules to see if anything will happen with the ions in solution.<span />
Atomic radius
Explanation:
A decrease in moving from the bottom of Group 3 to the top of the group shows an increase in trend from top to bottom.
The atomic radius of elements increases from top to bottom and decreases from the bottom to the top.
The elements in group 3 are B, Al , Ga, In and Tl
- Atomic radius is taken as half of the inter-nuclear distance between two covalently bonded atoms of non-metallic elements or half of the distance between two nuclei in the solid state of metals.
- Downs a group from top to bottom, atomic radii increases progressively due to successive shells being added.
- This compensates for the size reducing effect of the increased nuclear charge.
learn more:
Atomic radii brainly.com/question/5048216
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Answer:
no it does not fftyhhhhhhvvvv
hey there!:
A) Knowing theatre the protease is showing the highest activity at pH 4-6, implies that the amino acid that amino acid that it is acting in is an amino acid with a basic side chain. Therefore, the residues can be any one of the three basic amino acids being histidine, arginine or lysine , having basic side chains at neutral pH.
b) The mechanism of reaction of cysteine proteases is as follows:
First step in the reaction is the deprotonation of a thiol in the cysteine proteases's active site by an adjacent amino acid with a basic side chain, which might be a histidine residue. This is followed by a nucleophilic attack by the anionic sulfur of the deprotonated cysteine on the substrate carbonyl carbon.
Here, a part of the substrate is released with an amine terminus, restoring the His into a deprotonated form, thus forming a thioester intermediate, forming a link between the carboxy-terminal of the substrate and cysteine, resulting in thiol formation. Thus the name thiol proteases. The thioester bond is then hydrolyzed into a carboxylic acid moiety while again forming the free enzyme.
C) cysteine proteases have a pka of 8-9 but when they are deprotonated by a His residue, their pka would come down to 6-8, which would be their optimal pH for functioning. This is because there is a deprotonation of the thiol group , later restoring the HIS deprotonated form and then formation of a thioester bond. This thioester bond when hydrolysed will a carboxylate moeity , which is responsible for bringing the pH down towards a more acidic side.
d) at the optimal pH , the fraction of deprotonated cysteine and protonated B will be equal which will change with the change in pH.
Hope this helps!
