Category: CSIR NET Previous Year Questions Gel Electrophoresis

Category: CSIR NET Previous Year Questions Gel Electrophoresis

CSIR NET Previous Year Questions on Gel Electrophoresis – Video and Text Solutions by Let’s Talk Academy

Gel electrophoresis is one of the most frequently tested topics in the CSIR NET Life Science exam. It plays a critical role in molecular biology, helping to separate nucleic acids and proteins based on size and charge. To master this topic, practicing previous year questions (PYQs) is essential for understanding the pattern and improving accuracy.

Let’s Talk Academy, the leading institute for CSIR NET Life Science, provides comprehensive video and text-based solutions for gel electrophoresis questions, ensuring conceptual clarity and problem-solving accuracy.

Why Practice CSIR NET PYQs on Gel Electrophoresis?

Understanding the pattern and difficulty level of questions.
Identifying high-yield concepts and frequently repeated questions.
Strengthening theoretical and practical knowledge.
 Boosting confidence and accuracy in the exam.

Complete Solutions: Get clear explanations of past questions with proper techniques and tips.
Video and Text Format: Choose between video walkthroughs and text-based guides for convenient learning.
Expert Insights: Learn from experienced faculty who specialize in CSIR NET Life Sciences.

Boost your preparation and master blotting techniques with Let’s Talk Academy’s detailed solutions. Start preparing today and increase your chances of success in the CSIR NET Life Science exam!

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Cytochrome-C (MW 11.7 kD) and Myoglobin (MW 17.2 KD) are to be separated by polyacrylamide gel electrophoresis

Cytochrome-C and Myoglobin separated by polyacrylamide gel electrophoresis

Determination of the molecular weight by molecular exclusion chromatography

Determination of the molecular weight by molecular exclusion chromatography

radio-labeled nucleotides followed by urea PAGE

DNA replication with radio-labeled nucleotides, followed by urea-polyacrylamide gel electrophoresis (PAGE)

Determine Isoelectric point protein

To determine the Isoelectric point of a protein

Two-dimensional gel electrophoresis (2D-GE)

Two-dimensional gel electrophoresis (2D-GE)

To determine the Isoelectric point of a Protein, Isoelectric focusing

Determine the isoelectric point of a protein

To determine the Isoelectric point of a Protein, Isoelectric focusing

To determine the Isoelectric point of a Protein, Isoelectric focusing

Protein Separation Role of SDS Explained

SDS-PAGE & Protein Separation Role of SDS Explained

The electrophoretic mobility characteristics of migration of different biomolecules.

The electrophoretic mobility of migration of different biomolecules

In SDS PAGE of protein one SDS molecule will bind to

In SDS PAGE of protein one SDS molecule will bind to

Advantage of discontinuous buffer system in SDS and native PAGE

Advantage of discontinuous buffer system in SDS and native PAGE

tracking dye used SDS PAGE

Tracking Dye Used in SDS PAGE

Tracking Dye in SDS PAGE of Protein

Tracking Dye in SDS PAGE of Protein

Glycerol is Added to Protein Samples in Wells of PAGE

Glycerol is Added to Protein Samples in Wells of PAGE

In electrophoresis, protein will move until

In Electrophoresis Protein Will Move Until

Advantage of Difference in Gel Electrophoresis (DiGE)

Advantage of Difference in Gel Electrophoresis (DiGE)

Electrophoresis of Single Stranded DNA or RNA

Electrophoresis of Single Stranded DNA or RNA

If the amount of agarose added is more, the molecule under analysis should have following characteristic

Amount of agarose added is more Higher agarose concentration

How is the size of molecules under analysis measured

How is the size of molecules under analysis measured

The charge present on the DNA backbone is negative

The charge present on the DNA backbone is negative

Serum protein separated in agarose gel stained with Ponseau S stain

Serum protein separated in agarose gel stained with Ponseau S stain

Electroendosmotic flow disturb protein migration in the gel

Electroendosmotic flow disturb protein migration in the gel

Total charge of a protein in native gel is determined by the pH

Total charge of a protein in native gel is determined by the pH

2D gel electrophoresis Isoelectric Focusing (IEF) and SDS-PAGE

2D gel electrophoresis Isoelectric Focusing (IEF) and SDS-PAGE

Isoelectric Focusing (IEF)-The separation of proteins is only based on charge

Isoelectric Focusing-The separation of proteins is only based on charge

SDS PAGE separate proteins based on their molecular weight

SDS PAGE separate proteins based on their molecular weight

Free-Flow Electrophoresis (FFE) separates proteins based on their electrophoretic mobility in a free-flowing liquid medium rather than a gel.

Free flow electrophoresis-separated according to their electrophoretic mobility

SDS-PAGE -Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis

SDS-PAGE -Sodium Dodecyl Sulfate – Polyacrylamide Gel Electrophoresis

Isoelectric focusing (IEF) is a technique used in Two-Dimensional Gel Electrophoresis (2D-PAGE) as the first dimension to separate proteins based on their isoelectric point (pI)

The electrophoresis technique that use isoelectric focusing is

Two dimensional gel electrophoresis is a technique for separating proteins

Two dimensional gel electrophoresis is a technique for separating proteins

APS (Ammonium persulphate) is used in SDS-PAGE for

APS (Ammonium persulphate) is used in SDS-PAGE

In polyacrylamide gel electrophoresis (PAGE), molecules migrate based on size and charge. Free oligonucleotide Small and negatively charged → Moves fastest through the gel.

An oligonucleotide bound to a protein migrates slower than the free oligonucleotide in a polyacrylamide gel

Chymotrypsinogen in the native state and reduced unfolded sates is loaded- Gel-electrophoresis

Chymotrypsinogen in the native state and reduced unfolded sates is loaded- Gel-electrophoresis

Proteins A and B having a molecular weight of 16500 and 35400 move 1.3 cm and 4.6 cm

Proteins A and B having a molecular weight of 16500 and 35400 move 1.3 cm and 4.6 cm

The relative electrophoretic mobilities of a 30-kd protein and a 92-kd protein used as standards on an SDS

The relative electrophoretic mobilities of a 30-kd protein and a 92-kd protein used as standards on an SDS

What is an issue with using 2D-PAGE

What is an issue with using 2D-PAGE

SDS used in the electrophoresis of proteins- SDS coats the protein with a negative charge so that the sample can run through the gel

SDS Used in the Electrophoresis of Proteins

Gel Electrophoresis to work Negatively charged nucleic acids Agarose or polyacrylamide to separate Ethidium bromide (EtBr)

Important for Gel Electrophoresis to work

Northern blot analysis is used to detect specific mRNA in a sample Run the RNA through an oligo-dT affinity column

Prepare RNA for Northern blot analysis

Isoelectric focusing (IEF) separates proteins based on their isoelectric point (pI), which is the pH at which a protein has no net charge.

Isoelectric focusing separation of protein-on positive and negative

Approaches measure the mass of the purified protein complex and its subunit composition is Gel-filtration chromatography and Western blotting

Approaches is used to measure the approximate mass of the purified protein complex and to determine its subunit composition

Isoelectric focusing (IEF) separates proteins based on their isoelectric point (pI), which is the pH at which a protein carries no net charge.

Technique that can be used to analyze proteins-isoelectric focusing?

How can we pick a fragment of DNA from EtBr stained gel

Fragment of DNA from EtBr stained gel

DNA two different tubes where one has high G-C content cesium chloride density gradient

Identify the DNA two different tubes where one has high G-C content

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