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Genetics, Translation Chapter 13
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Biomedical Science notes that were made from the lectures given by Jan Kooter (Vu). Red lines signify importance or have a high possibility of being on the exam
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Start codon: AUG= methionineThe code degenerate: one codon can translate into multiple amino acids
Wobble base: the last base is usually the degenerate base
Code is universal (with exceptions)
Polypeptide=protein
N terminal: Amino terminal end, NH3 side
C terminal: Carboxyl terminal end, CO2 side
Binding
R group: sidechain amino acid
Hydrophobic: Non polar inside of the protein
Hydrophilic: polar on the outside of the protein
Primary structure: Linear sequence amino acid
Secondary structure: A- helix or B-sheet
A-helix: hydrogen bonds between amino acids
B-sheets: hydrogen bonds between proteins?
Tertiary structure: Mix of a-helix and b-sheets with unfolded parts that don’t influence the
function of the polypeptide
Quaternary structure: Protein complex of multiple protein subunits
tRNA: each bind a different amino acid and all have different names
Secondary structure tRNA: 3 stem loops (Variable region) and accepter stem (single strand
region)
tRNA: has modified bases (important for recognition for anticodon)
Accepter sequence: (ACC) bind amino acid
tRNA charging:
Wobble pairing: mismatches that can be tolerated
Isoaccepter tRNA: tRNA’s that can recognize the same codon
Ribosome: macromolecular complex
Bacteria only have 1 type
Eukaryotic cells have 2: one in cytoplasm, one in organelles (mitochondria chloroplast)
Svedberg units: rate at which subunit sediment when subjected to ultracentrifugation
Prokaryotic ribosome: 70S
small subunit: 30S
Large subunit: 50S
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