The correct answer is Introduction Quantitative analysis of enzyme inhibition is essential for both basic biochemistry research and drug development. The Dixon plot is a classic graphical method used to […]
Tag: csir enzyme kinetics
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Interpreting Enzyme Specificity Using Activity Profiles After Inhibitor and Heat Treatments
The correct answer is (3) Both X and Y are specific for the substrate, S. Introduction Substrate specificity is a key property for enzymes, defining their role in cellular metabolism and […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Analyzing Serine Protease Catalytic Efficiency and Substrate Binding: Insights from Peptide Length and Sequence
The correct answer is (1) A and B. Introduction Enzyme kinetics provide critical insights into how substrate structure influences catalytic efficiency and binding. Serine proteases, important for protein digestion, exhibit unique […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
pH Dependence of Enzyme Catalytic Efficiency: Role of Ionizable Residues in Catalysis
(DEC 2013 GU) 43. The Kcat/Km values of an enzyme-catalyzed reaction when plotted as a function of pH yielded a bell-shaped curve with a maximum around pH 6.0. Which of […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Comparing Catalytic Efficiency (kcat/Kmkcat/Km) from Enzyme Activity Curves: Analysis and Interpretation
The correct answer is (2) a > b > c. Introduction Catalytic efficiency (kcat/Kmkcat/Km) is a key measure in enzyme kinetics, representing how rapidly and effectively an enzyme converts substrate to […]
![(JUNE 2018) 36. The Vmax and Km from a Lineweaver-Burk plot of an enzyme reaction where 1/v = 40µM-1 min at 1/[S] = 0 and 1/[S] = -1.5 x 102 mM-1 at 1/v = 0 are (1) 0.025 µM min-1 and 0.67 x 10-2mM (2) 0.025 µM-1 min and 0.67 x 10-2 (3) 0.025 µM min-1 and 1.5 x 102 mM-1 (4) 0.038 µM min-1 and 0.67 x 10-2mM](https://www.letstalkacademy.com/wp-content/uploads/2025/09/36-1.jpg)
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Determining VmaxVmax and KmKm from a Lineweaver-Burk Plot: Step-by-Step Explanation
(JUNE 2018) 36. The Vmax and Km from a Lineweaver-Burk plot of an enzyme reaction where 1/v = 40µM-1 min at 1/[S] = 0 and 1/[S] = -1.5 x 102 […]
![(JUNE 2012) 33. A plot of V/[S] versus V is generated for an enzyme catalyzed reaction, and a straight line is obtained. Indicate the information that can be obtained from the plot. (1) Vmax and Km can be obtained only from a plot of 1/V versus 1/[S]. (2) Km/Vmax from the slope (3) Vmax and Km (4) only Km](https://www.letstalkacademy.com/wp-content/uploads/2025/09/33.jpg)
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Interpreting a Plot of V/[S]V/[S] vs. VV in Enzyme Kinetics: Extracting Km and Vmax
(JUNE 2012) 33. A plot of V/[S] versus V is generated for an enzyme catalyzed reaction, and a straight line is obtained. Indicate the information that can be obtained from […]
