Taking into account the definition of molarity, the molarity of a solution that contains 30 moles naoh in 0.80 liters of solution is 37.5 
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<h3>Definition of molarity</h3>
Molar concentration or molarity is a measure of the concentration of a solute in a solution and indicates the number of moles of solute that are dissolved in a given volume.
The molarity of a solution is calculated by dividing the moles of solute by the volume of the solution:
Molarity is expressed in units .
<h3>This case</h3>
In this case, you have:
- number of moles= 30 moles
- volume= 0.80 L
Replacing in the definition of molarity:
Solving:
<u><em>Molarity= 37.5 </em></u><em />
Finally, the molarity of a solution that contains 30 moles naoh in 0.80 liters of solution is 37.5 .
Learn more about molarity:
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Using the ideal gas equation:
pV = nRT
n = pV / RT
1atm = 101325Pa, so p = 10132500Pa
1L = 0.001m^3, so V = 0.050m^3
R = 8.214 (ideal gas constant)
T = 273K
Hence moles of CO2 = (10132500 * 0.050) / (8.314 * 273) = 223.2101553
Reaction ratio between oxygen and CO2 is 1:2
Hence moles of O2 = 223... / 2 = 112 moles (3sf)
How many grams of Cu would be needed to react with 2.0 mol HNO3?
<span>by the equation </span>
<span>3Cu + 8HNO3 --> 3Cu(NO3)2 + 2NO + 4H2O </span>
<span>2.0 mol HNO3 reacts with 3/8 ths as many moles of Cu = 0.75 moles of Cu </span>
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!
Answer:
0.6022×10²³ molecules
Number of moles = 0.1 mol
Explanation:
Given data:
Mass of HCl = 3.65 g
Number of molecules = ?
Number of moles = ?
Solution:
Number of moles:
Number of moles = mass/molar mass
Number of moles = 3.65 g/36.45 g/mol
Number of moles = 0.1 mol
Number of molecules:
1 mole of any substance contain 6.022×10²³ molecules
0.1 mol × 6.022×10²³ molecules/ 1 mol
0.6022×10²³ molecules
