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- 1. Multiple ChoiceIn Chromatography the retardation factor Rf are used for identification of components. A high Rf and a low Rt (retention time) mean the component has agreater affinity to the stationary phase in both TLC and HPLC.greater affinity to the stationary phase in TLC but a greater affinity for the mobile phase in HPLCgreater affinity to the mobile phase in TLC but a greater affininty for the stationary phase in HPLCgreater affinity to the mobile phase in both TLC and HPLC
- 2. Multiple ChoiceThe mobile phase in paper chromatography is typically aplasmasolidgasliquid
- 3. Multiple ChoiceThe substance in the mixture that has the greatest affinity for the mobile phase will travelfastestslowest
- 4. Multiple ChoiceThe retention factor is usedto zero the chromatography scaleto identify unknown compounds in a sampleto retain solventas a starting tool for chromatography
- 5. Multiple Choice
A characteristic feature of any form of chromatography is the ...
calculation of an Rf value for the molecules separated.
use of an inert carrier gas.
use of a mobile and a stationary phase.
use of molecules that are soluble in water.
- 6. Multiple Choice
Thin layer chromatography is
partition chromatography
electrical mobility of ionic species
adsorption chromatography
none of the above
- 7. Multiple Choice
Ion-Exchange chromatography:
separate and analyze compounds that can be vaporized without decomposition
Also known as Liquid-Solid Chromatography
Materials used are either cation or anion resins
Separation based on partition coefficient between 2 immiscible liquids
- 8. Multiple Choice
What type of chromatography is depicted by the illustration?
Gel Filtration Chromatography
Column Chromatography
HPLC
Thin Layer Chromatography
- 9. Multiple Choice
Which of the following methods could be used to check the molecular weight of your purified protein?
SDS-PAGE
Mass Spectrometry
Analytical SEC
All of above
- 10. Multiple Choice
To elute target proteins from an affinity chromatography matrix, which of the following conditions would be the most appropriate?
Low salt concentrations
High salt concentrations
Adding a soluble ligand which competes with the affinity tagged protein for binding to the column
Just keep washing buffer through the column, isocratic elution
- 11. Multiple Choice
What is the starting point for selection of a suitable IEX matrix for purification of a recombinant protein?
Prediction of isoelectric point (pI) from the amino acid sequence
Test protein binding to an IEX matrix at a range of pHs and salt concentrations
Test protein binding to a selection of anion and cation exchange matrices
Pass your sample through a preparative column and elute with a salt gradient
- 12. Multiple Choice
Which of these techniques is often considered a suitable "polishing" step in a protein purification strategy?
Affinity chromatography (AC)
Ion-exchange chromatography (IEX)
Hydrophobic interaction chromatography (HIC)
Size-exclusion chromatography (SEC)
- 13. Multiple Choice
You find that your protein sample loses activity during storage. What can you do about this?
Add an additional purification step
Use a protease inhibitor during purification steps
Perform each step as quickly as possible, in a cold-room
All of the above
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