Proteins and cellular transport Flashcards
Folding of protein
Done after translation. Physical properties of proteins dictate how it folds
Effect of protein folding on function
Tertiary and quaternary structure most important for function. E.g. if a receptor is the wrong shape a hormone is not able to bind. If the structure of the protein is not correct it will not function properly leading to diseas
Clustering
Occurs when there are polar and non-polar side chains. Polar side chains will be on the outside, as they are hydrophilic and the non-polar side chains will cluster in the centre because they are hydrophobic
Primary structure
linear sequence of amino acids in the polypeptide, amino acids will have different properties
Secondary structure
Local structures within the peptide chain, caused by hydrogen bonds. Classically they are alpha-helix (spiral structures) and beta pleated sheet (ribbon structures).
Tertiary structure
The folding of the secondary structure to form a 3d shape. Include hydrogen bonds, electrostatic interactions, van der waals attraction, hydrophobic interaction. Individually weak but collectively strong
Quaternary structure
Formation of a protein complex with two or more polypeptide chain. Can be a globular protein.
Quality control mechanism of the secretory pathway
1) The signal recognition particle (SRP) will bind to the ribosome and pause translation. The ribosome will have a specific N-terminal signal sequence.
2) The SRP bound ribosome binds to the SRP receptor on the surface of the RER.
3) The SRP drops off, the protein is now being fed into the lumen of the RER via the protein translocator, translation continues.
4) The protein is now in the secretory pathway.
5) In the RER the polypeptide chain will fold to form its tertiary structure and where post translational modifications will occur. Disulphide bonds will form.
Where do proteins synthesised from free ribosomes end up?
Cytosol, mitochondria, nucleus and peroxisome. Because proteins can not move back from the ER to these organelles.
Protein destination
Protein destination is dependent on the location of the ribosome during translation. Proteins are normally translated in the ribosomes in the cytosol unless signalled to go to the RER (if they have an N-terminus)
How do proteins travel from the RER to the organelle they are needed in
Proteins are transported in vesicles from the RER to the golgi apparatus. =They are then packed in vesicles, the protein signals where it needs to go. Part of the membrane of the organelle bud off into the vesicles containing our protein. The vesicles then fuse and release their cargo proteins into the destination organelle.
Exocytosis
Vesicles fuse with the plasma membrane and release their cargo outside the cell
Endocytosis
vesicles form at the plasma membrane to capture proteins and move them into the cell
What is intracellular fluid?
Fluid within cells. Accounts for two thirds of fluid
What is extracellular fluid?
Fluid outside cells. Accounts for a third of our body fluid, divided between interstitial and plasma fluid