<u>Answer:</u> The freezing point of solution is 5.35°C
<u>Explanation:</u>
The equation used to calculate depression in freezing point follows:
To calculate the depression in freezing point, we use the equation:
Or,
where,
Freezing point of pure solution = 5.5°C
i = Vant hoff factor = 1 (For non-electrolytes)
= molal freezing point elevation constant = 4.90°C/m
= Given mass of solute (naphthalene) = 2.60 g
= Molar mass of solute (naphthalene) = 128.2 g/mol
= Mass of solvent (benzene) = 675 g
Putting values in above equation, we get:
Hence, the freezing point of solution is 5.35°C
Answer:
I believe it is B (if you get it wrong it's my fault)
Body cells and tissues
They help give oxygen and other nutrients to keep you healthy
Hope this helps, Godbless :)
Answer:
Mass = 684.2 g
Explanation:
Given data:
Moles of Aluminium = 25.36 mol
Mass of Al = ?
Solution:
Formula:
Number of moles = mass/ molar mass
Mass = number of moles × molar mass
Molar mass of Aluminium = 27 g/mol
Now we will put the values:
Mass = 25.36 mol × 26.98 g/mol
Mass = 684.2 g
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!
