Precision will be reduced, but yield will be increased

Optimisation of a PCR reaction is often a compromise between the competing demands for precision, efficiency and yield. Although the specific effects may vary, generally, increasing the annealing temperature will increase non-specific primer binding and reduce precision. Increasing the length of the elongation phase will reduce the proportion of incomplete newly-synthesised strands and therefore increase yield. In this case, the potential effect on efficiency is unclear. Increasing the elongation phase would increase the reaction time, but the time taken to ramp down to a lower annealing temperature would be reduced.

Which of the statement is worng? Aminopetrin………s

#Question id: 10282

#I Life Science/ Life Sciences Group – I-V

In the glycolytic reaction one of the step is catalyzed by ATP-dependent phosphofructokinase is essentially irreversible, at the same step which one of the following enzyme used in gluconeogenesis, both of the enzymes are ATP dependent.

#Question id: 10282

#SCPH05 I Biotechnology

In the glycolytic reaction one of the step is catalyzed by ATP-dependent phosphofructokinase is essentially irreversible, at the same step which one of the following enzyme used in gluconeogenesis, both of the enzymes are ATP dependent.

#Question id: 10283

#I Life Science/ Life Sciences Group – I-V

How to Phosphofructokinase-1 (PFK-1) and Fructose 1,6-Bisphosphatase are reciprocally regulated ?

a) ATP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphate

b) citrate is also an allosteric regulator of PFK-1, high citrate concentration increases the inhibitory effect of ATP

c) FBPase-1, is strongly inhibited (allosterically) by AMP; when the cell’s supply of ATP is low (corresponding to high AMP), the ATP-requiring synthesis of glucose slows

d) AMP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphate

Which of the following statements of regulation of enzyme is correct?

#Question id: 10283

#SCPH05 I Biotechnology

How to Phosphofructokinase-1 (PFK-1) and Fructose 1,6-Bisphosphatase are reciprocally regulated ?

a) ATP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphate

b) citrate is also an allosteric regulator of PFK-1, high citrate concentration increases the inhibitory effect of ATP

c) FBPase-1, is strongly inhibited (allosterically) by AMP; when the cell’s supply of ATP is low (corresponding to high AMP), the ATP-requiring synthesis of glucose slows

d) AMP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphate

Which of the following statements of regulation of enzyme is correct?

#Question id: 10284

#I Life Science/ Life Sciences Group – I-V

Allosteric regulation of enzyme multisubunit or multiactive site shows cooperativity with the sigmoidal graph between substerate conc. v/s Activity,

a) Cell contain NADH, FADH2 and ATP, that inhibits the allosteric enzyme activity by lowering the affinity with its substate, graph shifts towards B from control

 b) A- shows low ATP, the Km for fructose 6-phosphate is relatively low, the affinity of the enzyme with its substate is relatively high

 c) Haemoglobin, Phosphofructokinase, Phosphate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, these all enzymes shows characteristics of sigmoidal graph

 d) When ATP is high, Km for fructose 6-phosphate is greatly increased- this activity shown by B in the graph

 e) fructose 2,6-bisphosphate binds to its allosteric site on PFK-1, it increases the enzyme’s affinity for its substrate fructose 6-phosphate and reduces its affinity for the allosteric inhibitors ATP and citrate- shown in graph by A

 Which of the following  combination of the enzyme activity with its substate correctly shown;

#Question id: 10284

#SCPH05 I Biotechnology

Allosteric regulation of enzyme multisubunit or multiactive site shows cooperativity with the sigmoidal graph between substerate conc. v/s Activity,

a) Cell contain NADH, FADH2 and ATP, that inhibits the allosteric enzyme activity by lowering the affinity with its substate, graph shifts towards B from control

 b) A- shows low ATP, the Km for fructose 6-phosphate is relatively low, the affinity of the enzyme with its substate is relatively high

 c) Haemoglobin, Phosphofructokinase, Phosphate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, these all enzymes shows characteristics of sigmoidal graph

 d) When ATP is high, Km for fructose 6-phosphate is greatly increased- this activity shown by B in the graph

 e) fructose 2,6-bisphosphate binds to its allosteric site on PFK-1, it increases the enzyme’s affinity for its substrate fructose 6-phosphate and reduces its affinity for the allosteric inhibitors ATP and citrate- shown in graph by A

 Which of the following  combination of the enzyme activity with its substate correctly shown;