(DEC 2006) 54. If an enzyme obeying Hills reaction shows negative cooperativity. It means (1) Binding of substrate to any one site of multi-subunit enzyme decreases affinity for other substrate […]
Tag: csir pyq biochemistry
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CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Modeling Oxygen Binding to Hemoglobin and Myoglobin: Kinetic Equations and Curve Fitting
The correct answer is (1) Myoglobin: curve A, reaction i, equations III and IV. Hemoglobin: curve B, reaction ii, equations I and II. Introduction Oxygen transport proteins in vertebrates—hemoglobin and myoglobin—exhibit […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Interpreting Sigmoidal Kinetic Graphs: The Signature of Cooperativity in Biology
The correct answer is (1) Cooperativity. Introduction Graphs in biological kinetics and molecular interactions reveal fundamental information about the mechanism and nature of biological processes. One of the most distinctive patterns […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Calculating Substrate Hydrolysis Rate for Pyrophosphatase Under Saturating Conditions
(DEC 2011) 49. The hydrolysis of pyrophoshate to orthophosphate is important for several biosynthetic reactions. In E. coli, the molecular mass of the enzyme pyrophosphatase is 120 kD and it […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Matching Enzyme Properties to Kinetic Expressions: A Guide to Biochemical Definitions
The correct answer is (3) A- iv, B- iii, C- ii, D- i. Introduction Enzyme kinetics is foundational for understanding biochemical reactions and enzyme activity. Properly identifying how various properties—such as […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Common Misconceptions in Enzyme Kinetics: Understanding Allosteric Behavior, Energy Change, Inhibition, and Catalytic Efficiency
(JUNE 2019) 47. Which one of the following statements is NOT correct? (1) Allosteric enzymes do not obey Michaelis-Menten kinetics. (2) The free-energy change provides information about the spontaneity but […]
CSIR NET Life Science Previous Year Questions and Solution on Biochemistry
Calculating Turnover Number and Kinetic Isotope Effect in Proton and Deuteron Transfer Enzyme Reactions
(NOV 2020-1) 46. An enzyme catalyzed reaction comparing proton and deuteron transfer reactions yielded the following kinetic data Kcat [H], s-1 70.7 KM [H], mM 1.03 Kcat [H], s-1 10.3 […]
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 […]
