Quality Control Of Proteins Flashcards
Quality control begins in the ….
ER
Genetic information ->
Functional proteins by transcription, translation, folding
Linear amino-acid chain ->
Unique functional structure
Folding intermediates, hydrophobic domains, aggregation prone
Describe the 4 structures of proteins
- Primary: The unique sequence of amino acids in the protein.
- Secondary : Coiling or bending of the polypeptide into an alpha helix or a beta pleated sheet. They can exist separately or jointly in a protein
- Tertiary: The folding back of a molecule upon itself and held together by disulfide bridges and hydrogen bonds. This adds to the proteins stability
- Quaternary: Complex molecule formed by the interaction of 2 or more polypeptide chains with various subunits
Protein folding leaves what in the core
Hydrophobic residues in an terror core
Burying hydrophobic residues in the interior core is…
Energetically favourable as it is the conformation of lowest free energy
If a protein ……….. on he surface it means it is …..
If a protein has a sizeable exposed patch of hydrophobic amino acids on its surface it is misfolded (abnormal)
What could cause a protein to be misfolded?
Failed to fold properly after it left the ribosome
An accident causes it to unfold
Failed to find its partner subunit on a larger protein complex
Misfolded proteins form…
Aggregates which are dangerous to the cell
what minimises the damage of misfolded proteins
Elaborate mechanisms that recognise the hydrophobic patches on proteins and minimise the damage they cause
Describe protein folding
Some protein folding begins immediately s the protein chain emerges from the ribosome, starting from the N-terminal end
As it emerges it forms a compact structure that contains most of the final secondary features in roughly the right conformation
For some protein domains this dynamic and flexible state called a molten globule is the starting point in which many side chain adjustments occur it takes several minutes to synthesise a protein of average size
For some proteins much of the folding process is complete by the time the ribosomes release the C-terminal end of the protein
most proteins require what to fold
Molecular chaperones
What are molecular chaperones?
Proteins that interact, stabilise or help a nonnative protein to acquire its native conformation
describe molecular chaperones
Not present in the final functional structure
Chaperones optimise the efficiency of folding
Without chaperones proteins may follow the wrong pathway and could aggregate
Specifically recognise incorrect off pathway proteins by their exposure of hydrophobic surfaces
Chaperones bind the hydrophobic surfaces of normal proteins to their own hydrophobic surfaces
In order to maintain homeostasis, the cell needs to remove:
Incorrectly synthesised proteins (errors in amino acid sequence)
Damaged proteins (oxidative damage)
Cell-cycle specific proteins
Signalling proteins no longer required