In chemical reactions the reactants are on the left side of the equation and the product are on the right
Answer:
Option D) Compound B may have a lower molecular weight.
Explanation:
Compound A and B are standing at the same temperature yet compound A is evaporating more slowly than compound B.
This simply indicates that compound B have a lower molecular weight than compound A.
This can further be seen when gasoline and kerosene are placed under same temperature. The gasoline will evaporate faster than kerosene because the molecular weight of the gasoline is low when compared to that of the kerosene.
The question is incomplete, here is the complete question:
How many grams of helium must be released to reduce the pressure to 65 atm assuming ideal gas behavior. Note : 334-mL cylinder for use in chemistry lectures contains 5.209 g of helium at 23°C.
<u>Answer:</u> The mass of helium released is 1.6 grams
<u>Explanation:</u>
We are given:
Mass of helium in the cylinder = 5.209 g
To calculate the number of moles, we use the equation given by ideal gas equation:
PV = nRT
Or,
where,
P = Pressure of the gas = 65 atm
V = Volume of the gas = 334 mL = 0.334 L (Conversion factor: 1 L = 1000 mL)
w = Weight of the gas = ?
M = Molar mass of helium gas = 4 g/mol
R = Gas constant = 
T = Temperature of the gas = ![23^oC=[23+273]K=296K](https://tex.z-dn.net/?f=23%5EoC%3D%5B23%2B273%5DK%3D296K)
Putting values in above equation, we get:
Mass of helium released = (5.209 - 3.573) g = 1.636 g = 1.6 g
Hence, the mass of helium released is 1.6 grams
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!
Yo!
Im not sure 'bout your answer but 60 percent the answer can be,
The body could take in too much dietary fiber, which harms the cell.
