Tag: GATE Life Science Previous Year Papers with Solutions

Q.42 Shown below is an electrospray ionization mass spectrum of a protein:The numbers written on top of the peaks are the m/z values. The mass of the protein deduced fromthe […]

Q.41 One litre of phosphate buffer was prepared by adding 208 grams of Na2HPO4 (Mol. wt. 142) and 71 grams of NaH2PO4 (Mol. wt. 120) in water. If the pKa […]

Q.40 The kinetic data for a single substrate enzyme is shown below. The concentration of inhibitor [I] used in the reaction was equal to the Ki of the inhibitor. The […]

Q.39 Match the entries in Group I with those in Group II Group I P) J chain Q) Serpin R) β2-microglobulin S) Artemis Group II 1) VDJ recombinase complex 2) […]

Q.38 The concentration of Mg2+ ions outside a cell is twice the concentration inside. If the transmembrane potential of the cell is −60 mV (inside negative), the free energy change […]

Q.37 A purified oligomeric protein was analyzed by SDS-PAGE under reducing and non-reducing conditions. A one litre solution of 1 mg/ml concentration has 4.01 × 1018 molecules of the oligomeric […]

Q.36 An aqueous solution contains two compounds X and Y. This solution gave absorbance values of 1.0 and 0.4 at 220 and 280 nm, respectively, in a 1 cm path […]

Q.35 Given below is the hydropathy plot of a monomeric transmembrane protein.How many transmembrane α–helices are present in the protein?(A) 1 (B) 2 (C) 4 (D)5 What is Given A […]

Q.34 Consider the following biochemical reaction:Fructose 6–phosphate + ATP Fructose 1,6–bisphosphate + ADPThe equilibrium constant under biochemical standard conditions (K’eq) for the above reaction is 254.The standard free energy change […]

Q.33 For a single substrate enzyme, a reaction is carried out at a substrate concentration four times thevalue of Km. The observed initial velocity will be _________ % of Vmax. […]