otro2 Flashcards

1
Q
A
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2
Q

Where does translation start in prokaryotes and eukaryotes? Describe the process.

A

The ribosome attaches its two units to the
mRNA and begins to read it from the 5’ to the 3’ end until it reaches the start codon ( AUG,GUG,UUG) ( AUG Met)
The start codon is preceded by a whole initiation complex , in the middle of which is a purine-rich sequence :
ÿ Prokaryotes: Shine-Dalgarno sequence
ÿ Eukaryotes: Kozak sequence

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3
Q

Name at least two antibiotics and/or toxins that inhibit protein synthesis and briefly describe the mechanism.

A

Streptomycin: inhibits initiation (inhibits binding of fMet-rTRNA) and thus causes a
incorrect reading of mRNA
Tetracycline: binds to the 30 subunit and inhibits the attachment of the aminoacyl-tRNA

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4
Q

What is the typical structure of eukaryotic transcription factors? Name three typical DNA binding structures.

A

Transcription factors bind to specific sections of DNA and regulate how much messenger RNA (mRNA) is produced
from it (transcription rate).
1.DNA-binding domain:
2.Activation domain: initiates transcription through interactions with RNA Pol II and/or its associated proteins or
through local changes in chromatin structure
DNA-binding structures in eukaryotic transcription factors:
-* Homeodomain (helix-turn-helix)
* Leucine zipper domain (bZip domain)
* Zinc finger domains

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5
Q

The binding of oxygen depends on the oxygen partial pressure:

A
  • high O2 partial pressure: protein is oxygenated > R-form
  • low O2 partial pressure, no O2 bound > T-shape
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5
Q

e Bohr effect

A

describes the decrease in the affinity of hemoglobin (Hb) to oxygen when the pH value decreases
or the CO2 concentration increasesThe lower the pH value, the easier H+ is absorbed and O2 is released.

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6
Q

Types of enzyme regulation: Explain how the enzymatic activity of proteins can be regulated. Give one
example of each.

A
  1. Allosterische Regulation - Aspartat Transcarbamoylase
    Activator molecules occupy the allosteric center and thus cause a conformational
    change:
  2. Regulation with Isoenzyme - LDH-Formen: M4-Isoenzym, H4-Isoenzym
  3. Regulation by covalent modification - histones in DNA packaging
  4. Activation by proteolytic cleavage - pepsin in the stomach, trypsin in the pancreas
  5. Activation by co-activators – CoA, metal ions
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