A) SrBr2
b) C3P4
c) Be3(PO4)2
dCa3P2
e) MnS2O3
d) NO
Answer:
A protein has four subunits whose molecular masses are 140, 80, and 60 kDa.
A disulfide bond links the two 80 kDa subunits (possibly identical).
Explanation:
Given that:
A protein has four subunits whose molecular masses are 140, 80, and 60 kDa.
A disulfide bond links the two 80 kDa subunits (possibly identical).
As a result of SDS and dithiothreitol analysis treatment, the molecular masses can not be 360 in total. They are 280, which implies that they are in short of 80 kDa. This means that there are possibilities that two groups with a molecular mass of 80 kDa which are joined by a disulfide bond.
The presence of SDS and dithiothreitol acts as a reducing agent, and they can break disulfide bonds whose pH is greater than 7, i.e. those in basic condition.
Answer:
The steps with correct mechanism are given below:
C
1) CH₄(g) + Cl(g) → CH₃(g) + HCl(g) : This is a slow step.
The rate is given as: R1 = k₁[CH₄][Cl]
2) CH₃(g) + Cl₂(g) → CH₃Cl(g) + Cl(g): This is a fast step.
The rate is given as: Rate = k₂[CH₃][Cl₂]
∴ CH₄(g) + Cl₂(g) → CH₃Cl(g) + HCl(g)
Here, the slowest step will be the rate-determining step.
In 3.8 moles of li, there are about <span>0.144071459 grams. I assume that you are talking about lithium.</span>
7 A lead
B Gold
Csilver
8 Afeathrr
B water
C silver
