June 2025 - Page 37 of 114

Explain the Strain and Distortion catalysis mechanism of enzyme. Describe reversible covalent modification of enzymes for regulating enzyme activity.

Strain and Distortion Catalysis and Reversible Covalent Modification of Enzymes Part A: Strain and Distortion Catalysis Mechanism Introduction Enzymes enhance reaction rates through various catalytic mechanisms. One such mechanism is strain or distortion catalysis, where the enzyme alters the structure of the substrate to resemble the transition state. This structural change lowers the activation energy […]

Explain the Strain and Distortion catalysis mechanism of enzyme. Describe reversible covalent modification of enzymes for regulating enzyme activity. Read More »

Derive Michaelis-Menten equation for an uncompetitive inhibitor.

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Derivation of Michaelis-Menten Equation for an Uncompetitive Inhibitor Introduction Uncompetitive inhibition is a type of enzyme inhibition where the inhibitor binds only to the enzyme-substrate (ES) complex and not to the free enzyme. This form of inhibition decreases both the maximum velocity (Vmax) and the Michaelis constant (Km) of the enzyme-catalyzed reaction, but their ratio

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Differentiate between: a) Ordered and Random mechanism for Bisubstrate reactions. b) Ligases and Lyases

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Key Differences in Enzyme Mechanisms and Classes a) Ordered vs. Random Mechanism for Bisubstrate Reactions Introduction Bisubstrate reactions involve two different substrates interacting with an enzyme. The sequence in which the substrates bind to the enzyme is vital in understanding the reaction mechanism. Two common types are the Ordered mechanism and the Random mechanism. Ordered

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Explain Fischer Lock and Key Hypothesis. Derive Lineweaver Burk equation from Michaelis Menten equation.

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Fischer Lock and Key Hypothesis and Derivation of Lineweaver-Burk Equation Part A: Fischer Lock and Key Hypothesis Introduction The Fischer Lock and Key Hypothesis is one of the earliest models proposed to explain the specificity of enzymes for their substrates. Introduced by Emil Fischer in 1894, this theory is a cornerstone of enzyme-substrate interaction models

Explain Fischer Lock and Key Hypothesis. Derive Lineweaver Burk equation from Michaelis Menten equation. Read More »

Give an overview of transition state theory of enzyme and describe the effect of pH on enzyme activity.

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Overview of Transition State Theory and Effect of pH on Enzyme Activity a) Transition State Theory of Enzyme Action Transition state theory is a concept in chemistry and enzymology that explains how enzymes catalyze chemical reactions. It states that chemical reactions proceed through a high-energy intermediate state called the transition state. Enzymes function by stabilizing

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Write short note on the following terms: a) Characteristics of Enzymes b) Apoenzyme c) Coenzyme d) Turnover number

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Short Notes on Key Enzyme Terminologies a) Characteristics of Enzymes Enzymes are biological catalysts that speed up chemical reactions without being consumed in the process. Key characteristics include: Specificity: Each enzyme acts on a specific substrate due to the unique shape of its active site. Efficiency: Enzymes can greatly accelerate reactions, often by a million

Write short note on the following terms: a) Characteristics of Enzymes b) Apoenzyme c) Coenzyme d) Turnover number Read More »

BBCCT-105 – Proteins Assignment Master Post

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BBCCT-105 – Proteins Assignment Master Post Below are the links to all the answers for the assignment questions under the course code BBCCT-105 – Proteins. Define amino acids and classify them based on their chemical structure and properties. Discuss the significance of peptide bonds in protein structure. Include an explanation of how peptide bonds are

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A. Draw Ramachandran plot and explain it importance. B. Explain the N-terminal protein sequencing method

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Ramachandran Plot and N-terminal Protein Sequencing Method Part A: Ramachandran Plot Definition: A Ramachandran plot is a graphical representation that shows the possible combinations of dihedral angles (phi φ and psi ψ) of amino acids in a protein structure. It helps visualize allowed and disallowed conformations due to steric hindrance. Diagram: Importance: Helps in validating

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Explain the mechanism of action of contractile proteins like actin and myosin in muscle contraction. What structural features enable their function?

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Mechanism of Action of Contractile Proteins: Actin and Myosin Introduction Muscle contraction is a vital biological process that allows movement and stability in the human body. This process is driven by the interaction of two main contractile proteins: actin and myosin. These proteins work together in a repeating cycle to produce contraction and relaxation in

Explain the mechanism of action of contractile proteins like actin and myosin in muscle contraction. What structural features enable their function? Read More »

Describe the role of storage proteins such as ferritin and ovalbumin in biological systems. How do their structures support their functions?

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Role of Storage Proteins and How Their Structures Support Their Functions Introduction Storage proteins are essential biomolecules that store vital nutrients, such as amino acids and metal ions, for use during periods of demand. Two well-known examples of storage proteins are ferritin and ovalbumin. Their structures are closely related to their functions in living organisms.

Describe the role of storage proteins such as ferritin and ovalbumin in biological systems. How do their structures support their functions? Read More »