OK, another classification of proteins depends on the number of segments that

cross the membranes. So here we are talking only in this case In the left side of
the slide we are talking about Trans membrane protein, also called integral
membrane proteins. We can distinguish between the single pass protein meaning it
pass so without the membrane on the ones meaning that it's just one transmembrane
segment in these proteins. In the second time we have two examples of multi pass
transmembrane proteins. It means that if we analyse the sequence of this protein,
we can identify at least two segments that are typically embedded in the membrane.
In this case, for example, we have a multipass transmencement protein with seven
different Helix that represent the seven different segments across the membrane.
The other example of transmembrane protein in this case this is a channel. Instead
of using Helix, we use a beta bar structure made-up by beta strands. The result is
the same. We have sort of a channel in which the structure of the channel is made-
up by strengths beta strands and there are a number of them, I think at least 10 or
12. So this is a multi pass transplant protein with at least 12 different segments
that cross the membranes. On the right side of this slide, we have two example of
peripheral proteins. In this case, we don't have a transmembrane protein that
brings the peripheral protein to the membrane. So these are two examples that are
different from the example that was shown in the previous slide. Here for example,
we have a Helix that can associate from one side to the membrane and on the other
side, the other side face the cytosol. So we can say that probably in this Helix
there are a number of residues that can contact the polar heads of lipids while the
other side of the Helix face the cytosol. This is a a non covalent interaction from
with the with the membrane. Remember non covalent interaction on the other side.
There are a number of loops that can contact the lipids of the membranes while the
remaining part of the protein is outside. This is quite typical. The orientation of
membrane proteins remain constant. Remember the concept of flip flop of lipids? We
know that even though at low rate 1 lipid can change its location inside the
membrane. So change from 1 leaflet to the other, move from 1 leaflet to the other
flip is called the process that goes from the cytosol to the exoplasmic phase. The
flop movement is the reverse. Proteins never do the flip flop inside the membrane.
It's impossible for the protein to do this first because it's too big. It can't
happen for lipids because they have a polar head which is highly hydrofilmed. But
it's not that big as a protein in this case. If we can see that, for example, this
protein to make a flip flop of this object, we should be able to bring inside the
membrane all the extracellular portion of the protein. If something is something
face the cytosol or face the extracellular environment, it must be an hydro, an
hydrophilic portion of the protein, because we have amino acids that are constantly
in contact with water. So we expect to have a number of residues in the red portion
of this protein, both the big one, the small a number of residues that are highly
polar because these are residues in the portion of the protein that are in constant
contact with water. So we should move all these amino acids inside the membrane in
order to cross the membrane and give the possibility to this portion to face the
other side of the cell. And this is impossible to do. We don't have an enzyme that
is able to flip flop a protein. So once a protein is synthesized in the specific
orientation inside the membrane, that orientation will. Remain the same through all
the life of the protein. The same thing regard peripheral proteins. If a proteins
is peripheral, if a protein a peripheral protein phase the cytosol, that
orientation will remain the same during all the life of the protein. If a protein
must be exposed to the extracellular environment, being a peripheral protein again,
the protein will remain there and we will never have the opportunity to change its
orientation in the plasma membrane. So basically once they are synthesised, they
remain in the place where they have been put the first time. Peripheral proteins
for example. Here we have two examples of proteins peripheral that binds A
transmembrane segment. This case we have two proteins that are lipidated. So
example five shows a protein which is lipid anchored protein which is inserted in
the cytosolic leaflet of the membrane. The other example is a protein which is
lipidated again and it is exposed to the exoplasmic leaflets of the membrane. There
is a detail more here. Those structures that are blue, they are carbohydrates.
Several proteins that are in the exoplasmic phase of the membrane are usually are
modified with carbohydrates. So if we know that the membrane protein is modified by
additional carbohydrates, we can be sure that that protein would be exposed to the
exoplasmic phase of the membrane, not the cytoplasmic. 1. Sugars are always
outside, OK Seven and eight are two examples of peripheral proteins that binds.

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