Answer:
in a solution of salt in water, the solute is salt, and solvent is water.
Explanation:
C) salt is the solute, water is the solvent.
Lithium Hydroxide (LiOH) is an Arrhenius base
B. At the equivalence point of a titration of the [H+] concentration is equal to 7.
<h3>What is equivalence point of a titration?</h3>
The equivalence point of a titration is a point in titration at which the amount of titrant added is just enough to completely neutralize the analyte solution.
At the equivalence point in an acid-base titration, moles of base equals moles of acid and the solution only contains salt and water.
At the equivalence point, equal amounts of H+ and OH- ions combines as shown below;
H⁺ + OH⁻ → H₂O
The pH of resulting solution is 7.0 (neutral).
Thus, the pH at the equivalence point for this titration will always be 7.0.
Learn more about equivalence point here: brainly.com/question/23502649
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Answer:
aldehyde
carbon-1
ketone
carbon-2
Explanation:
Monosaccharides are colorless crystalline solids that are very soluble in water. Moat have a swwet taste. D-Fructose is the sweetest monosaccharide.
In the open chain form, monosaaccharides have a carbonuyl group in one of their chains. If the carbonyl group is in the form of an aldehyde group, the monosaccharide is an aldose; if the carbonyl group is in the form of a ketone group, the monosaccharide is known as a ketose. glucose is an aldose while fructose is a ketose.
In D-glucose, there is an aldehyde functional group, and the carbonyl group is at carbon-1 when looking at the Fischer projection.
In D-fructose, there is a ketone functional group, and the carbonyl group is at carbon-2 when looking at the Fischer projection.
Answer:
True
Explanation:
In an uncompetitive inhibition, initially the substrate [S] binds to the active site of the enzyme [E] and forms an enzyme-substrate activated complex [ES].
The inhibitor molecule then binds to the enzyme- substrate complex [ES], resulting in the formation of [ESI] complex, thereby inhibiting the reaction.
This inhibition is called uncompetitive because the inhibitor does not compete with the substrate to bind on the active site of the enzyme.
Therefore, in an uncompetitive inhibition, the inhibitor molecule can not bind on the active site of the enzyme directly. The inhibitor can only bind to the enzyme-substrate complex formed.
