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
The answer is:
The rate constant K2 = 1.9 x 10^-4 1/s
The explanation:
According to Arrhenius equation:
ln(k₁/k₂) = Ea/R (1/T₂ - 1/T₁)
when K is the rate constant
and Ea is the activation energy
R is the ideal gas constant
T1 & T2 is a temperature at kelvin
when we have:
Ea = 272 KJ = 272000 J
R is the ideal gas constant 8.3145 J/Kmol
K1 = 2.3 x 10^-5 1/s K2 = ?? that is we need to calculate
T1 = 718 K T2 =753 K
So by substitution:
ln(k₁/k₂) = Ea/R (1/T₂ - 1/T₁)
㏑(2.3X10^-5/K2) = [272000/8.314](1/753-1/718)
∴ K2 = 1.9 x 10^-4 1/s
Answer:
False.
Explanation:
Hello there!
In this case, according to the attached picture, it is possible for us to evidence that cis- isomers have the substituted groups on the same side of the double bond whereas the trans- isomers have the substituted groups on the opposite side of the double bond.
In such a way, we infer that the given statement is FALSE, because that is the definition for the trans configuration.
Regards!
Answer:
1:2
Explanation:
For every 4 moles of aluminum, there are 2 moles of aluminum oxide, so the mole ratio when converting from aluminum to alunmimum oxide is
2 moles aluminum oxide:4 moles aluminum. This can be simplified to 1:2.
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