2D Gel Electrophoresis of the Egg Proteins
1. In a 2D gel where each spot represents a protein of a particular pI value and molecular weight, what will be your inference about two proteins whose positions are horizontal to each other in the gel?:
2. If you perform electrophoresis of histones and myoglobins having pI 8.5 and 5.5 respectively, under denaturing conditions at pH 7.0, what will be the migration pattern of these proteins? :
3. Why is mineral oil added over the IPG strips during rehydration?
4. In which buffer are the IPG strips equilibrated first before the second-dimension separation?
5. What temperature is maintained during isoelectric focusing?
6. What type of gel is typically used for the second dimension in SDS-PAGE?
7. Which step in the 2D gel electrophoresis procedure ensures that proteins are denatured and coated with a uniform negative charge?
8. Which type of proteins can be analyzed using 2D gel electrophoresis?
9. How are proteins visualized after SDS-PAGE?
10. What is the typical pH range of IPG strips used for isoelectric focusing?