membrane proteins Flashcards
four major classes of lipids
phospholipids- ester bonds
sterols- cholesterol
sphingolipids - major in neuronal membrane
primary found in plasma membrane
glycolipids- found on the outside of cell
synthesised in ER/golgi
what causes the classic bilayer
POPC
conical
hexagonal phase
maximises hydrophobic out and
hydrophilic in
vesicles support conical bilayer
micelle shape
hydrophobic roots are on the inside
overall shape of lipid effects what
phase adapted
bilayer structure
x-ray/ neutron diffraction facts
doesnt need to be a crystal
can use on any repeated pattern
scatter tells us the spacing between repeated structures
waves get scattered when it hits the bilayer
what law do they follow
Braggs law:
n(lambda)=2dsin (thita)
d is spacing
influence of bilayer on protein structure
4 points
protein must interact with hydrophobic bilayer core
must cope with changes in environment at bilayer surface
bilayer highly dynamic, but solid interface required from both protein and bilayer integrity
must provide architecture to carry out its function
membrane protein structure
what do you consider
thermodynamics
maximise h-bonds to get the lowest free energy
what happens when inserting protein sidechains into the bilayer?
-ch3 and -ch2
will cause vdm giving us hydrophobic port
key points for membrane protein
maximise the number of hydrogen bonds
choose your aa sequence carefully
secondary structure of membrane proteins
what do they achieve
no N-h or carbonyl groups that are unpaired
maximising the number of H-bonds
alpha helical transmembrane domains
what do the side chains provide
all side chains are pointing away from core of the helix
interacts with bilayer
length of alpha helical TM domains
each AA gives a rise of 1.5A
bilayer about 36A long
so at least 24 residues to cross the bilayer
acyl chains that are shorter make the bilayer thinner
hydrophobic aa are located in the hydrophobic core on the membrane what are they
ala
val
leucine
isoleucine
aromatic residues what do they provide
around head group
because they are amphipathic they can change switch from hydrophobic to phillic
what aromatic residues are they
phenylalanine
tysosine
tryptophan
positive inside rule
arg and lys
found on the inside
helix packing
what are the crossing angles
-37
+83
+22
TM helical packing normally occurs between
+5 and +25
antiparallel packing preferred
helix interactions promoted by
small sidechain:
spacially Gs are 1 above each other
- maximises interactions between species
- this causes a gap
helix interactions promoted by
polar residues:
generates stable interactions between 2 TM domains
identification between membrane proteins
kyte-doolittle plots
based on hydrophobicity of aa
what does the 7 regions of hydrophobicity give us
they give us 7 regions of TM domains