Translation of mRNA - The relationship between the genetic code and protein synthesis
22 important questions on Translation of mRNA - The relationship between the genetic code and protein synthesis
Which 4 different codons are there?
- Start codon (AUG, methionine).
- Stop codon (UAA, UAG, UGA), aka termination codons or nonsense codons.
- mRNA also contains untranslated regions (not translated into a protein), thd 5'-untranslated region and 3'-translated region.
How many different amino acids are there, and how many different codons, and what is the result of the answers?
- Different codons: 4^3 = 64
Therefore, multiple codons specify for the same amino acid.
GGU, GGC, GGA, and GGG all specify the amino acid glycine. How are such codons called?
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What is the reading frame?
Is the genetic code in all organisms the same?
Which amino acids are sometimes called the twenty-first and twenty-second amino acids?
Which codons encode for selenocysteine and pyrrolysine?
How is selenocysteine incorporated in the polypeptide (instead of the binding of release factors for termination)?
- This SECIS region is recognized by proteins that favor the binding of selenocysteine instead of release factors.
How is pyrrolysine incorporated in the polypeptide (instead of release factors for termination)?
- Which are recognized by proteins that favor the binding of a pyrrolysine.
How are the amino acids in a polypeptide connected, and between which groups of the amino acids?
How is the reaction, in which a polypeptide is made out of amino acids, called? And which molecule is released?
How is the first amino acid of a polypeptide called (so the first added one)?
Which part of an amino acid determines the particular chemical properties of the amino acid?
What does nonpolar and polar mean on how an amino acid reacts to water?
- Polar means they are hydrophilic.
Where in a folded protein would you more likely find a hydrophobic amino acid? And where would you find a hydrophilic amino acid?
Is an polypeptide often found in a lineair structure.
What is the secondary structure of a polypeptide?
Does the whole polypeptide have the same secondary structure, or is it just a part?
Which regions in the polypeptide make the molecule able to fold?
Why does the folding of a polypeptide occur spontaneously?
By which interactions is the structure of a polypeptide determined?
- Ionic interactions among charged amino acids;
- Hydrogen bonding among amino acids in the folded polypeptide;
- Weak bonds known as van der Waals interactions.
What is the quaternary structure of a protein?
- When the polypeptides in one protein interact with each other, they form a quaternary structure.
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