These are proteins that binds a trans membrane protein.

So this association is
mediated by protein protein interactions, protein protein interactions. One example
of single plasma protein is glycophorin A, which is a dimeric protein. What does it
mean? It means that once it is synthesizing the oblasting reticulum 2 subunits
associate one with the other, they make a dimer. And we will always see this
protein like a dimeric structure, never a single monomer as all the transmembrane
protein, in particular the single past transmembrane protein. This protein has a
quite short intracellular domain, in this case the carboxyl terminal, and is in the
cytosol. Outside we have big extracellular portion and then we have one chiliate
that cross the membrane. The external part of the protein is highly modified by
additional carbohydrates. This is a protein that can be found in the membrane of
red blood cells, and usually red blood cells contained a lot of carbohydrates on
the surface that are used to modify the membrane proteins of this cell. So if we
look at the residues that typify the intracellular portion and the extracellular
portion, as we said before, we will find here a lot of polar and charged amino
acids. But what happens to the Helix that cross the membrane? What kind of residues
do we have do we expect to see? Here we have a Helix and the R groups members that
the R groups of the Helix are polar not polar. If you have to cross the membrane
you cannot use polar residues. OK, so these two Helix are full of non polar amino
acids. If you have the sequence on your desk, the sequence of this protein,
probably you could be able to identify the segments corresponding to the
hydrophobic portion of the membrane of the protein simply looking at the
composition. Because when we say that the Helix hydrophobic is completely
hydrophobic, we have something like about 20 amino acids, 1 after the other and
none of them is a polar or charged amino acid. So it's quite easy to identify
stretches of amino acid across the membrane. The other example of transmembrane
protein is a protein called porine. We have not discussed about the function of
porine, but we have a slide that we have mentioned in the last week that one week
ago approximately in which we talk about Gram positive and gram negative bacterial
cells. And we said that gram negative have these properties to have two membranes
instead of 1. So we have a plasma membrane then layer which is thin of
peptidoglycan. Remember that this is full of carbohydrates and also proteins. But
then we have also a second layer which is another membrane. So if we don't put the
structure to the structure of a gram positive bacterial cell, of course the surface
of the upper one is completely hydrophilic because it's made-up by A thick layer of
the glycan that can capture big quantities of water. So we expect that this
bacterial cell is full of water outside on the other case. In this case we have
outside the layer which is made-up of lipids. So it's completely different the
surface of this bacterial cell. It is completely hydrophobic, but if it is
hydrophobic, it means that water will cross its membrane, but at a very lower rate
compared to the other example. And indeed, it's not strange that in these bacterial
cells in the outer membrane we find a lot of chlorines, which are transmembrane
proteins made-up by a beta barrel that are able to they allow the water to cross
the external layer of the membrane. So the advantage of having a lot of pourines in
these membranes is the fact that the bacterial cells can capture water from the
outside, even though there is a value of lipids. The structure of pourines is this.
We have seen this picture more than one time. This is a beta bar and remember the
number of beta strands that fold like a shit making a cylinder? We have a number of
hydrophobic residues with peak R groups made-up by cyclic reams. They usually are
in the interface between lipids and the cytosolic portion of the membrane of the
yes, the membrane. So this is the beta barrel and it is a channel for water. And in
the native confirmation pita barrel 11 porine is associated with two other porine.
They make a trimmer in each of these channels water or greasal ore can pass. They
are also useful for the uptake of desaccharide ions and other small molecule, but
mainly water lipid anchors. We said that there are at least three kinds of anchors
that can be added to a protein in order to make it a a sort of peripheral membrane
protein. The first case, the first modification is called acceleration. These kinds
of modification are called lipidation. In the first case we add an acid group,
basically a hydrocarbon chain, a long lipid which is this one that alone a light
allow the association of the protein with the membrane. Another modification is
called pronulation. This is pronulation, it is the additional pharmacy or generally
generally groups. They are like hydrocarbon chains but they are branches because we
have here number of ramifications. Anyway, you we don't need to memorize the
structure of this.

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