Answer:
A noncompetitive inhibitor can only bind to an enzyme with or without a substrate at several places at a particular point in time
Explanation:
this is because It changes the conformation of an enzyme as well as its active site, which makes the substrate unable to bind to the enzyme effectively so that the efficiency of the enzyme decreases. A noncompetitive inhibitor binds to the enzyme away from the active site, altering/distorting the shape of the enzyme so that even if the substrate can bind, the active site functions less effectively and most of the time also the inhibitor is reversible
I can't answer this question without knowing what the specific heat capacity of the calorimeter is. Luckily, I found a similar problem from another website which is shown in the attached picture.
Q = nCpΔT
Q = (1.14 g)(1 mol/114 g)(6.97 kJ/kmol·°C)(10°C)(1000 mol/1 kmol)
<em>Q = +6970 kJ</em>
ok so i think it would be b because gravity would pull you down but your the same size
Hey there!
Given the reaction:
B + H⁺ => HB⁺
At half-equivalence point : [B] = [HB⁺]
=> [B] / [HB⁺] = 1
Henderson-Hasselbalch equation :
pH = pKa + log ( [B] ) / ( HB⁺)]
pH = 14 - pKb + log ( 1 )
pH = 14 - 7.95 + 0
pH = 6.05
Answer C
Hope that helps!
