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#Question id: 565


A transition-state analog:

#Section 2: General Biology
  1. is less stable when binding to an enzyme than the normal substrate.

  2. resembles the active site of general acid-base enzymes.

  3. resembles the transition-state structure of the normal enzyme-substrate complex.

  4. stabilizes the transition state for the normal enzyme-substrate complex.


Answer:- Option(s): 3


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#Question id: 604

#Section 2: General Biology

An enzyme is irreversibly inhibited by diisopropylfluorophosphate (DFP). What does this show?

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#Question id: 605

#Section 2: General Biology

Which statement is false about allosteric regulation?

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#Question id: 606

#Section 2: General Biology

Which statement is false about regulatory enzymes that are controlled allosterically?

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#Question id: 607

#Section 2: General Biology

In E. coli ________ is an activator and ________ is a negative allosteric modulator of the enzyme phosphofructokinase-1. 

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#Question id: 608

#Section 2: General Biology

The ʺTʺ state refers to the ________.

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#Question id: 609

#Section 2: General Biology

The ________ theory explains cooperative binding by suggesting all subunits of a given protein have the same conformation, either all R or all T.

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