L13: Revision & prokaryotic protein synthesis Flashcards
Sequence of AA in protein
Held together by covalent bonds (peptide bonds)
Read from amino terminus to carboxyl terminus
Unique characteristic of every protein
Encoded by nucleotide sequence of DNA
Side groups
Affect protein structure and function
Example: hydrophobicity. Tryptophan and glutamine
Protein structure
Secondary structure: folding; alpha helix
Tertiary structure: packing; polypeptide chain
Quaternary structure: interaction; assembled subunits
Example of when primary sequence affect protein function
In normal Hb: has Glu -> not hydrophobic
In sickle Hb: has Val -> hydrophobic, no polarity -> change in structure of Hb -> sickle shape
Translation
Occurs in cytoplasm
Complex process- requires >300 molecules in eukaryotes
mRNA- used as template to guide synthesis of chain of AA -> protein
Protein synthesis occurs at ribosomes. Ribosomes composed of RNAs (rRNA) & proteins
tRNA delivers AA to synthesise polypeptide chain
Polycistronic mRNA
Carry several open reading frames . Each of which can be translated into polypeptide
Eukaryotic mRNA
Monocistronic
Contains genetic info to translate single protein chain (polypeptide)
Ribosomes
Protein biosynthesis occurs by process of translation on ribosomes
Prokaryote: ribonucleoprotein particles found in cytosol of all cells. 20,000 ribosomes in cell, 20% of cell’s mass. 70S ribosome (2 subunits: 50S, 30S). Composed of RNA and protein.
Eukaryote translation
Electron micrograph of polysomes
Multiple ribosomes translating same mRNA
Ribosomes move toward 3’ end of mRNA
Proteins synthesised N-terminal to C-terminal