Tag: GATE Life Science Previous Year Papers with Solutions

Q.43 A polypeptide with the amino acid sequence ‘AGKPDHEKAHL’ was dissolved in a buffer of pH 1.8. The predominant form of the polypeptide will have a net charge of (A) […]

Q.42 Kinetic parameters for the enzyme fumarase with three different substrates are given below. Substrate                                […]

Q.41 Aspartate residues are found in the active sites of many enzymes. The 𝐩𝐊𝐚 for the 𝜷-carboxylate of aspartate is 3.86 . At physiological pH this group can function as […]

Q.40 An enzyme was purified using ion-exchange chromatography and the results are shown in the table below. Step                          […]

Q.39 Three micrograms of a circular plasmid of 4200 bp was digested with a restriction enzyme and subjected to agarose gel electrophoresis. Five DNA fragments of different sizes were observed […]

Q.38 When freshly isolated intact mitochondria were incubated with ADP and inorganic phosphate neither the oxygen consumption nor the ATP synthesis could be detected. Addition of succinate resulted in increased […]

Q.37 The 𝚫𝐆′𝐨for the malate dehydrogenase catalyzed step of Krebs cycle is +𝟕. 𝟏𝐤𝐜𝐚𝐥/𝐦𝐨𝐥𝐞.Nevertheless, the conversion of malate to oxaloacetate in vivo proceeds spontaneously because the subsequent reaction that consumes […]

Q.36 Four groups of metabolites are given below. Choose the group in which all the compounds contain at least one bond whose 𝚫𝐆′𝟎 of hydrolysis is ≤ −𝟕. 𝟎𝐤𝐜𝐚𝐥/𝐦𝐨𝐥𝐞. (A) […]

Q.35 Polypeptides are biosynthesized on the ribosomes inside the cell. Chemical synthesis of polypeptides is also possible through Merrifield’s solid-phase peptide synthesis. In both the cases the polypeptide chain is […]

Q.34 The fluidity of a phospholipid membrane increases when the fatty acid (A) chain length increases and degree of unsaturation decreases (B) chain length decreases and degree of unsaturation increases […]