Protein Structure and Translation Flashcards
Transcription occurs in the
Nucleus
Primary Structure (Protein)
Amino Acid chain and order
Amino Acid
20 different kinds incorporated into proteins, and it has to be incorporated into a protein to be considered an amino acid.
Secondary Structure (Protein)
Results from interactions in nearby amino acids.
A-helices and B pleated sheets
Tertiary Structure (Protein)
3-dimensional shape of a polypeptide, hydrophobic and hydrophilic interactions, H-bonding, Disulfide bridges.
Quaternary Structure (Protein)
Results from interactions of polypeptide subunits.
Special Amino Acids
Glycine, Proline, Cysteine
Glycine
Allows for rotation
Proline
Allows for rigidity
Cysteine
SH groups cause disulfide bonding, hold 3-dimensional shape
Peptide bond
Formed by dehydration synthesis, links carboxyl end to the amine end
Alpha Helix
Each carboyl group in the backbone forms an H-bond with an amine group four residues away.
Beta Pleated Sheet
Adjacent strands can run in the same direction or in opposite. Hydrogen bonds form between carbonyl groups in one polypeptide and amide groups in a different part of the polypeptide.
Aminoacyl tRNA synthetases
Charge tRNA with the correct amino acid
Ribosome structure
Large subunit and small subunit. Large subunit has the exit site, the peptidyl site, and the aminoacyl site.