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Novay_Z [31]
3 years ago
10

Select the true statements about SDS‑PAGE, a method of separating proteins. Assume that SDS‑PAGE is performed under reducing

conditions.
a. Proteins are separated in a polyacrylamide gel matrix.
b. Protein‑SDS complexes have similar mass to charge ratios; therefore, separation is by size.
c. Proteins are visualized using a dye that binds to the gel matrix, but not to proteins.
d. Smaller proteins migrate faster through the polyacrylamide gel.
e. Sodium dodecyl sulfate binds proteins, resulting in protein‑SDS complexes that are similar in size.
f. Protein‑SDS complexes migrate toward the negative electrode.
Chemistry
1 answer:
Tanzania [10]3 years ago
6 0
Proteins are separated
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Explain why the place of aluminum in the reactivity wagon seems to be unsuitable.
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2 years ago
Using the data, which of the following is the rate constant for the rearrangement of methyl isonitrile at 320 °C? (HINT: the act
algol13

Answer:

D) 2.3 x 10⁻¹ s⁻¹

Explanation:

The rate constant is related to the activation energy through the formula:

k= Ae^(-Eₐ /RT)

where A is the collision factor, Eₐ the activation energy, R is the gas constant ( 8.314 J/Kmol ) , and T is the temperature (K)

So a plot of lnk versus 1/T ( Arrehenius plot ) gives us a straight line with slope equal -Eₐ/R and intercept lnA

lnk = -(Eₐ/T)(1/T) + lnA

which has the form y= mx + b

In this problem, we can use the data provided to:

a) Using a calculator determine the slope and intercept and then calculate the value of rate constant at 320 ºC, or

b) Plot the data and determine the equation of the best line , and answer the question for k @ 320 ºC by reading the value from the plot.

Once you do the plot, the resulting equation is:

y = - 19 x 10³ x + 30,582 ( R² = 0.999 )

So for T = 320 + 273 K = 593 K

Y = 19 x 10³ X + 30.58

So for T = (320 + 273)K = 593 K

Y =  -19 x 10³ ( 1/593) + 30.58 = -32.04 +30.58 = - 1.46

and then since

y = lnk ⇒ e^y = k

k= e^-1.46 = 2.3 x 10⁻¹ s⁻¹

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