TLS Online TPP Program

#Question id: 3788


The spontaneous loss of amino groups from adenine in DNA results in hypoxanthine, an uncommon base, opposite thymine. What combination of proteins could repair such damage?

#Section 3: Genetics, Cellular and Molecular Biology
  1. nuclease, DNA polymerase, DNA ligase

  2. telomerase, primase, DNA polymerase

  3. telomerase, helicase, single-strand binding protein

  4. DNA ligase, replication fork proteins, adenylyl cyclase

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TLS Online TPP Program

#Question id: 3009

#Section 2: General Biology

 Endospores are

TLS Online TPP Program

#Question id: 413

#Section 4: Fundamentals of Biological Engineering

The hydrolysis of ATP has a large negative DG'°; nevertheless it is stable in solution due to:

TLS Online TPP Program

#Question id: 27344

#Section 5: Bioprocess Engineering and Process Biotechnology

In a chemostat, evaluate the dilution rate at the cell wash-out condition by applying Monod's model with the given set of data: μmax = 1 h-1; YX/S = 0.5 g g-1; Ks = 0.2 g/L; S0 = 10 g/L

TLS Online TPP Program

#Question id: 14860

#Section 4: Fundamentals of Biological Engineering

A fermentation slurry containing Streptomyces kanamyceticus cells is filtered using a continuous rotary vacuum filter. 120 kg h- 1 slurry is fed to the filter; 1 kg slurry contains 60 g cell solids. To improve filtration rates, particles of diatomaceous-earth filter aid are added at a rate of 10 kg h- 1. The concentration of kanamycin in the slurry is 0.05% by weight. Liquid filtrate is collected at a rate of 112 kg h-1; the concentration of kanamycin in the filtrate is 0.045% (w/w). Filter cake containing cells and filter aid is continuously removed from the filter cloth.
 What percentage liquid is the filter cake?

TLS Online TPP Program

#Question id: 4152

#Section 3: Genetics, Cellular and Molecular Biology

The pathway for polypeptides exported from E. coli includes the following steps, which occur in what order for correct export?

1.  A chaperone, SecA, binds to the polypeptide.

2.  A chaperone, SecB, binds to the polypeptide.

3.  ATP is hydrolyzed by Sec A.

4.  SecA pushes 20 amino acids of the polypeptide into the translocation complex.