1. Figure out a problem
2. Research
3. Hypothesis
4. Experiment
5. Analyze results
6. Conclusion
7. Communicate your results
Hope This Helps. :D <span />
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.
The theoretical proportion is given by the balanced chemical equation:
2 mol NBr / 3 mol Na OH
Then x mol NaOH / 40 mol NBr3 = 3mol NaOH/2 mol NBr3
Solve for x, x = 40 * 3/2 = 60 mol NaOH.
Given that there are 48 mol NaOH (less than 60) this is the limitant reactant and the other is the excess reactant.
Answer: NBr3..
<span> There are 97.2 mol of O in 10.8 mol of Fe(NO3)3</span>
