If the temperature of the sample of gas increases to the given value, the volume also increases to 600mL.
<h3>What is Charles's law?</h3>
Charles's law states that "the volume occupied by a definite quantity of gas is directly proportional to its absolute temperature.
It is expressed as;
V₁/T₁ = V₂/T₂
Given the data in the question;
- Initial temperature of gas T₁ = 100K
- Initial volume of gas V₁ = 300mL
- Final temperature T₂ = 200K
V₁/T₁ = V₂/T₂
V₂ = V₁T₂ / T₁
V₂ = ( 300mL × 200K ) / 100K
V₂ = 60000mLK / 100K
V₂ = 600mL
Therefore, if the temperature of the sample of gas increases to the given value, the volume also increases to 600mL.
Learn more about Charles's law here: brainly.com/question/12835309
#SPJ1
The bubbles indicate that there is a gas dissolved in the liquid, which may remain dissolved when the liquid is very cold, inside the refrigerator.
When the temperature of the liquid increases, it reduces its ability to dissolve the gas and the gas escapes (bubbles) from the liquid.
At the end, the behavior of the liquid permits you to conclude that the liquid is a mixture because it has a gas dissolved in it.
Answer:
No.
Explanation:
Mercury is not a solution. It is a detonator.
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!
