TLS Online TPP Program

#Question id: 2122


The inner (plasma) membrane of E. coli is about 75% lipid and 25% protein by weight.  How many molecules of membrane lipid are there for each molecule of protein?  (Assume that the average protein is Mr 50,000 and the average lipid is 750.)

#Unit 2. Cellular Organization
  1. 1

  2. 50

  3. 200

  4. 10,000

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TLS Online TPP Program

#Question id: 4479

#Unit 3. Fundamental Processes

The stepwise assembly of the Pol II preinitiation complex

TLS Online TPP Program

#Question id: 4480

#Unit 3. Fundamental Processes

The reason for TBP’s unorthodox recognition mechanism is

TLS Online TPP Program

#Question id: 4481

#Unit 3. Fundamental Processes

Choose correct statements about recognition mechanism of TBP ;

A. TBP causes the minor groove to be widened to an almost flat conformation

B. It also bends the DNA by an angle of ~120o

C. The interaction between TBP and DNA involves maximum number of hydrogen bonds between the protein and the edges of the base.

D. Much of the specificity is imposed by two pairs of phenylalanine side chains that intercalate between the base pairs at either end of the recognition sequence and drive the strong bend in the DNA.

TLS Online TPP Program

#Question id: 4482

#Unit 3. Fundamental Processes

The General Transcription Factors of RNA Polymerase, with their subunits, select correct matching

A.     TBP

      1

B.     TFIA

      11

C.     TAFs

       2

D.     TFIIH

      10

TLS Online TPP Program

#Question id: 4483

#Unit 3. Fundamental Processes

TAF42 and TAF62 from Drosophila form a structure similar to that of the

TLS Online TPP Program

#Question id: 4484

#Unit 3. Fundamental Processes

Match General Transcription Factors with their functions;

    i. TAFs

 A. Appears to regulate the binding of TBP to DNA. It does this using an inhibitory flap that binds to the DNA-binding surface of TBP, another example of molecular mimicry. This flap must be displaced for TBP to bind TATA.

  ii. TFIIB

B. Insert into the RNA-exit channel and active center cleft of Pol II in a manner analogous to the sigma region 3/4 linker in the bacterial case.

  iii. TFIIH

 C.  As an ATP-driven translocator of double-stranded DNA.

   iv. TFIIF

D. This two-subunit (in humans) factor associates with Pol II and is recruited to the promoter together with that enzyme.