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Protein purification

Total questions: 15

Worksheet time: 8mins

Name
Class
Date
1.

Protein purification refers to the:

a)

Purification of different cellular components

b)

The process of converting proteins into their primary structure

c)

The process of separating and isolating a specific protein from a complex mixture

d)

The process of denaturing proteins.

2.

●Protein separation techniques are often based on the following properties except

a)

Solubility of protein

b)

Viscosity of protein

c)

Charge  of the protein

d)

Specific binding affinity of the protein

3.

●In which of the following separation method where proteins are separated based on their net charge

a)

Affinity chromatography

b)

Ion exchange chromatography

c)

Dialysis

d)

Gel filtration chromatography

4.

●In gel filtration chromatography, the separation of proteins is based on their

  

a)

Size and net charge

b)

Size and shape

c)

Size and specific affinity

d)

Shape and net charge

5.

●The use of insulin hormone to purify its receptor is an example of

a)

Ion exchange chromatography

b)

Affinity chromatography

c)

Gel filtration chromatography

d)

none of the above

6.

In anion exchange chromatography

a)

The column contains negatively charged beads where positively charged proteins binds

b)

The column contains positively charged beads where negatively charged proteins bind

c)

The column contains both positive and negatively charged beads where proteins bind depending on their net charge

d)

All of these

7.

The best method to hydrolyzed tryptophan  is

a)

Acid hydrolysis

b)

Base hydrolysis

c)

Salting out

d)

Enzymatic hydrolysis

8.

●For the study of a protein in detail, an effort is usually made to first,

a)

Conjugate the protein to a known molecule

b)

Determination of amino acid composition

c)

Determination of amino acid sequence

d)

Purify the protein

9.

What is the primary purpose of using an internal standard in an HPLC method?

a)

To increase the separation efficiency of the HPLC column

b)

To enhance the sensitivity of the HPLC detector.

c)

To monitor and correct for variations in sample preparation, injection volume, and detector response.

d)

To decrease the retention times of analytes on the HPLC column.

10.

What is the primary benefit of using pre-column derivatization in HPLC for amino acid analysis?

a)

It reduces the need for sample preparation.

b)

It reduces the separation of amino acids on the HPLC column.

c)

It allows for direct detection of native amino acids.

d)

It enhances the sensitivity and selectivity of detection.

11.

Phenylisothiocyanate (PITC ) AA derivatives can be detected through:

a)

UV-visible spectroscopy

b)

visible light detection

c)

By fluorescent detector

d)

none of the above

12.

The time taken by the analyte after sample injection to reach the detector is called _________

a)

Dead time

b)

Solute migration rate

c)

Adjusted retention time

d)

Retention time

13.

In a chromatographic separation, which of the following is most appropriate for the qualitative analysis of a substance?

a)

Area of the component peak

b)

retention time

c)

dead time

d)

capacity factor

14.

In which chromatography stationary phase is more polar than the mobile phase?

a)

ion exchange chromatography

b)

Revered phase chromatography

c)

normal phase chromatography

d)

size exclusion chromatography

15.

Which of the following statements is true when comparing internal standards and external standards in HPLC for amino acid detection?

a)

Internal standards are never used in amino acid analysis.

b)

External standards provide a direct measurement of amino acid concentrations.

c)

Internal standards are added to the sample, while external standards are injected separately.

d)

External standards are always preferred over internal standards for accuracy.