Category: CSIR NET Previous Year Questions and Solutions on Stability of Proteins and Nucleic Acids

Category: CSIR NET Previous Year Questions and Solutions on Stability of Proteins and Nucleic Acids

CSIR NET Previous Year Questions on Stability of Proteins and Nucleic Acids – Video and Text Solutions by Let’s Talk Academy

Stability of Proteins and Nucleic Acids is one of the most important Biochemistry topic of CSIR NET Life Science exam. Practicing CSIR NET Previous Year Questions (PYQs) on Stability of Proteins and Nucleic Acids helps candidates understand the question patterns, improve accuracy, and strengthen conceptual clarity.

Let’s Talk Academy (LTA), the leading institute for CSIR NET Life Science, provides detailed video and text-based solutions to Stability of Proteins and Nucleic Acids-related PYQs, ensuring thorough understanding and problem-solving skills.

Why Focus on Stability of Proteins and Nucleic Acids PYQs for CSIR NET?

Stability of Proteins and Nucleic Acids is a high-weightage topic in CSIR NET Life Science.
Understanding Stability of Proteins and Nucleic Acids mechanisms and applications is essential for solving conceptual and application-based questions.
Practicing previous year questions helps to identify common patterns and improve accuracy.
Complete Solutions: Get clear explanations of past questions with proper techniques and tips.
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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!

18. Heating of some nucleic acids shows an increase in the absorbance at 260 nm (A260) typified by the plot shown above. The sharp transition midpoint is defined as melting temperature (Tm). Which one of the following nucleic acid samples is NOT expected to generate such a typical profile upon heating of its solution? (1) Double stranded DNA (2) Double stranded RNA (3) DNA:RNA hybrid DNA:RNA (4) Single stranded DNA having imperfect secondary structures

Understanding DNA Melting Profiles: Why Single-Stranded DNA with Imperfect Secondary Structures Lacks Typical Melting Curves

17. Double stranded DNA can be destabilized and denatured by (1) Formamide (2) Polyglycine (3) Sucrose (4) PEG

How Double-Stranded DNA Is Denatured: The Role of Formamide and Other Agents

Understanding Differences in DNA Denaturation Profiles: Role of GC Content and Genome Complexity

15. The graph between the concentration of Single stranded DNA (Y-axis) and decrease in temperature (X- axis during renaturation of DNA can be represented as

Which Graph Represents Single-Stranded DNA Concentration vs Decreasing Temperature During Renaturation?

14. The Temperature of Melting (Tm) is defined as the temperature at which 50% of double stranded DNA is changed to single-standard DNA. Tm of DNA does not depends on (1) Length of DNA (2) % GC content (3) Presence of cations (4) Presence of anions

 Understanding DNA Melting Temperature (Tm): Which Factor Does Not Influence It?

13. It has been observed that for the DNA double helix melting, the value of ΔH (enthalpy change of denaturation) are 80 and 90 kcal/mole at 700 and 800, respectively. Assuming that ΔCP (constant-pressure heat capacity change) is independent of temperature, estimate ΔH associated with the denaturation of DNA at 370C. This estimated value of ΔH (kcal/mole) is (1) 27 (2) 37 (3) 47 (4) 57

 How to Calculate DNA Denaturation Enthalpy (ΔH) at 37°C from Values at Higher Temperatures

12. Protein stability is represented as Prior to development of sensitive calorimeters, thermodynamic parameters of processes were determined by following equation ΔHO and ΔSO are standard changes m enthalpy and entropy, respectively. Which one of the following statements is correct for estimating ΔG, ΔH and ΔS? (1) Determining the ratio of folded and unfolded protein at 370C (2) Plotting Keq as a function of ΔH (3) Plotting Keq against ΔS (4) Plotting Keq against temperature

How to Estimate Protein Stability Thermodynamics Using Equilibrium Constant and Temperature

11. Differential scanning calorimetric study of calf thymus DNA was carried out to measure midpoint of thermal denaturation (Tm). ΔHm (enthalpy change at Tm) and ΔCP (constant-pressure heat capacity change). It has been observed that ΔCP =O, Tm =75.50C and ΔHm=50.4 kcal/mole. The Gibbs free energy change at 370C is (1) 25.5 kcal/mole (2) 2.6 kcal/mole (3) 0.6 kcal/mole (4) 5.6 kcal/mole

How to Calculate Gibbs Free Energy Change (ΔG) of DNA Denaturation at 37°C from DSC Data

10. Sodium dodecyl sulphate (SDS) denatures protein by altering their (1) Primary structure only (2) Primary and secondary structure (3) Secondary and tertiary structure (4) Primary, secondary and tertiary structure

 Understanding SDS-Induced Protein Denaturation: Effects on Secondary and Tertiary Structures

9. Most effective protein denaturant form of guanidinium when used in equimolar concentration is (1) Iodide (2) Chloride (3) Bromide (4) Sulphate

Which Guanidinium Salt Is the Most Effective Protein Denaturant? Understanding the Role of Counterions

8. A protein in 100 mM KCl solution was heated and the observed Tm (midpoint of unfolding) was 600C. When the same protein solution in 500 mM KCl was heated, the observed Tm was 650C. What is the most probable reason for this increase in Tm? (1) Hydrophobic interaction is increased and electrostatic repulsion is decreased. (2) Hydrophobic interaction is decreased and electrostatic repulsion is increased. (3) Hydrogen-bonding is increased. (4) van der Waals interaction is increased

How Salt Concentration Influences Protein Stability: Increased Hydrophobic Interaction and Reduced Electrostatic Repulsion Raise Tm

7. Globular protein when treated with organic solvent get denatured. The main interaction which is affected on treatment with organic solvent is (1) Hydrogen bonds (2) Covalent bonds (3) Ionic interactions (4) Hydrophobic interactions

Understanding Protein Denaturation by Organic Solvents: Hydrophobic Interactions Are Mainly Affected

6. Values of Tm (midpoint of denaturation), ΔHm (enthalpy change at Tm) and ΔCP (constant-pressure heat capacity change) of a protein are measured in a differential scanning calorimeter. ΔGD(T), the Gibbs free energy change at any temperature T(K) can be estimated using the following form of the Gibbs-Helmholtz equation with the values obtained from these measurements: The stability curve for the protein simulated using the observed thermodynamic values is given below: The shape of the stability curve is due to (1) hydrogen-bonding and electrostatic interactions only. (2) van der Waals and electrostatic interactions only. (3) only electrostatic interactions. (4) only hydrophobic interaction.

 What Determines the Shape of Protein Stability Curves? The Crucial Role of Hydrophobic Interactions

Interpreting Hydrogen Bond Angles in Protein Structures

Solubility of Protein X in Solutions of Ammonium Sulfate

Investigating the Stability of Proteins Under Different Conditions

The Stability of Proteins: Implications of Amino Acid Replacement

How Glycerol Stabilizes Solutions of Proteins

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