Cramming Flashcards
What is the most common lipid in membranes?
Phosphoglycerides
Describe phospholipids.
Amphipathic
Asymmetrical
What is spontaneous aggregation dependent on?
Fatty acid length
Temperature
Degree of saturation
What property of membranes does cholesterol enhance?
Fluidity
What are liquid ordered regions resistant to?
Non-ionic detergents
What are stored in lipid droplets?
Triglycerides and cholesterol esters
What is phospholipase A2 an example of?
Peripheral protein
How are lipid anchored proteins attached?
N-terminal glycine attached to fatty acyl group such as palmitate or myristate
What is an example of an energy independent flippase?
ER Flippases
What is an example of an energy dependent flippase?
Inward: P4 P-type ATPase
Outward: ABC transporters
How are soluble proteins and membrane proteins transported?
Signal based
How are integral proteins and plasma membrane proteins transported?
Vesicle based targeting
Where is the signal sequence located?
N-terminal
Describe ER signal sequences.
6-12 hydrophobic amino acids
16-30 residues long
One or more positive residues near the N-terminus
Describe the SRP.
6 proteins bound by 300nt of RNA - P54 subunit of the SRP contains a hydrophobic cleft which binds to the hydrophobic amino acids of the signal sequence.
What complex forms the mammalian translocon?
Sec61
What could the signal peptidase recognise?
A, C, G, T and S (-1 and -3)
What does Sec61/BiP do?
Prevents the polypeptide chain from slipping back into the cytosol.
BiP is a HSP protein that is located in the ER lumen - it contains a peptide binding domain and an ATPase domain that binds to and stabilises particularly or unfolded proteins.
Sec62 hydrolyses BiP.ATP causing a conformational change in BiP allowing it to bind to the polypeptide chain.
Describe type I integral proteins.
Cleaved N-terminal sequence, luminal N-terminal and cytosolic C-terminal.
Stop-transfer anchor
Describe type II integral proteins.
No cleavable N-terminus.
C-terminal luminal and N-terminal cytosolic
Signal anchor sequence
Positive charges on the N-terminal side
Describe type III integral proteins.
Same orientation as type I but no cleavable N-terminal - positive charges lie on the cytoplasmic side (C-terminal side)
Positive-inside rule = positive charged residues present on the cytoplasmic side.
Describe type IV.
Multiple transmembrane domains - mixture of stop-anchor and signal anchor sequences.
Can have either orientation.
Describe type V.
Linked to an amphipathic phospholipid anchor embedded in the membrane - attached by covalent amphipathic molecule - GPI. Small sequence of amino acids near the N-terminus is recognised and cleaved off by a transamidase and linked to the pre-formed GPI membrane anchor.
What is the sugar molecule in N-linked glycosylation attached to?
Nitrogen on an asparagine molecule