MH₂CO₃: (1g×2) + 12g + (16g×3) = 62 g/mol
1 mol --- 62g
0,8 mol -- X
X = 0,8×62
X = 49,6g
Answer:
molecular weight (Mb) = 0.42 g/mol
Explanation:
mass sample (solute) (wb) = 58.125 g
mass sln = 750.0 g = mass solute + mass solvent
∴ solute (b) unknown nonelectrolyte compound
∴ solvent (a): water
⇒ mb = mol solute/Kg solvent (nb/wa)
boiling point:
- ΔT = K*mb = 100.220°C ≅ 373.22 K
∴ K water = 1.86 K.Kg/mol
⇒ Mb = ? (molecular weight) (wb/nb)
⇒ mb = ΔT / K
⇒ mb = (373.22 K) / (1.86 K.Kg/mol)
⇒ mb = 200.656 mol/Kg
∴ mass solvent = 750.0 g - 58.125 g = 691.875 g = 0.692 Kg
moles solute:
⇒ nb = (200.656 mol/Kg)*(0.692 Kg) = 138.83 mol solute
molecular weight:
⇒ Mb = (58.125 g)/(138.83 mol) = 0.42 g/mol
2: <span>Volume V = a*b*c = 6.0*3.0*3.0 = 54.0 cm^3 density ρ = mass/volume = 146/54 = 2.70 g/cm^3
3: Volume = (27.8 -21.2) cm^3
mass = 22.4 g
density = 22.4/(27.8-21.2) g/cm^3
</span>
Answer:
The correct answer is: The substitution altered the secondary and tertiary structure of the enzyme so that the mutated enzyme folds into a different shape than the normal enzyme does.
Explanation:
In the given condition, the substitution mutation of gene causes a replacement of serine by phenylalanine amino acids which causes a reduction in the activity of the enzyme. Since serine is polar and has -OH or hydroxy group involves the information of binding of biological catalyst to the substrate.
The primary structure of a protein is significant which finalizes the number of amino acids their sequence. The mutation of protein also affects both secondary and tertiary structures as it disturbs the structure of the protein and affects the catalytic activity as well as the binding affinity of the substrate.
the substitution of serin by phenylalanine does not affect or influence the mass of enzyme.
2AgNO3+K2CrO4⇒Ag2CrO4(s)+2KNO3
Hence by mixing 0.0024M AgNO3 and 0.004M
K2CrO4, we will have Ag2CrO4 which is precipitated out and leave us with
0.0024M KN03 which is mixed with (0.004-0.0024/2)M, it can be 0.0028M, of K2Cr04