TLS Online TPP Program

#Question id: 32137


The degrees of freedom in the sugar–PO4 backbone of DNA chain is/are

#Unit 1. Molecules and their Interaction Relevant to Biology
  1. 1
  2. 3
  3. 4
  4. 7
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TLS Online TPP Program

#Question id: 1120

#Unit 4. Cell Communication and Cell Signaling

A mutation that knocks out the GTPase activity of a G protein would have what effect on a cell?

TLS Online TPP Program

#Question id: 19014

#Unit 13. Methods in Biology

Chromatography with solid stationary phase is called_________

TLS Online TPP Program

#Question id: 27483

#Unit 1. Molecules and their Interaction Relevant to Biology

Compounds which have the same molecular formula and sequence of bonded elements, but which are nonsuperimposable, non-mirror images

TLS Online TPP Program

#Question id: 4453

#Unit 3. Fundamental Processes

Correct statements about regions of the s70 factor which can be divided into four regions called s region 1 through s region 4;

TLS Online TPP Program

#Question id: 10284

#Unit 6. System Physiology – Plant

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;