Biomolecules (B)

Camels have three different sub-classes of $\operatorname{IgG}(\operatorname{IgG} 1, \operatorname{IgG} 2$ and $\operatorname{IgG} 3)$, of which IgG2 and IgG3 are structurally different from the human IgG. A researcher…

Depicted in the figure are three possibilities of substrate (white triangle) conversion to the product (gray triangle) by an enzyme (blue) in the presence of different kinds of reversible inhibitors. The corresponding…

Identify the non-reducing disaccharide:

The graph depicts energy diagram (potential energy vs progress of reaction) of an uncatalyzed (black solid line) and enzyme-catalysed (red solid line) biochemical reaction. Based on this information, consider the…

Analyze the images and deduce the correct structural description of the molecules.

A researcher determined the initial velocity $\left(\mathrm{V}_0\right)$ of an enzyme in three different reactions (corresponding to lines $\mathbf{P}, \mathbf{Q}$ and $\mathbf{R}$ in the graph) with increasing…

Proteins in biological systems are polypeptides that are exclusively made from Lamino acids. A peptide, $\mathbf{P}$, with L-amino acids of a particular sequence always adopts a right-handed alpha helical structure.…

Height of a plant is positively determined by the amount of final product, K, of a metabolic pathway catalyzed by five enzymes $L, N, P, M$ and $O$ (as depicted below). The intermediate product, $\mathbf{I}$, blocks the…

Monomeric subunits of proteins can sometimes assemble into higher order assemblies. Two such related human proteins $\mathbf{P}$ and $\mathbf{Q}$ assemble into hexamers by sequential assembly of their subunits. However,…

Trypsin is a digestive enzyme of serine protease group. It is considered an endopeptidase, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of…

A scientist performed enzyme kinetics and obtained velocity $\mathbf{v}$ as a function of substrate concentration $[\mathbf{S}]$ and the values are given in the table below. The $\mathrm{K}_m$ of the substrate could be

The graph given below shows the Michaelis-Menten kinetics for two reactions ($R_{1}$ and $R_{2}$; represented as solid and dotted lines, respectively). Enzymes $E_{1}$ and $E_{2}$ have $V_{\max }$ values, $V_{\max 1}$…