This blog intends to display concepts, informations, musics, videos, games, cartoons, curiosities about biochemical issues. Because Biochemistry does not have to be incomprehensible...
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- Fatty acids metabolism
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- Lipoproteins
- Aminoacids metabolism
Saturday, March 29, 2014
Thursday, March 27, 2014
Tuesday, March 25, 2014
Saturday, March 22, 2014
Lipoproteins (general considerations)
Despite the
high heterogeneity found among lipids, either in terms of their different
classes (fatty acids, triglycerides, cholesterol, cholesterol esters and
phospholipids), or even within each of these classes, there is a feature common
to all of them - its high insolubility in water. Indeed, although some of the
lipids have an amphipathic behavior (phospholipids and cholesterol) they are
predominantly apolar. Since in our body it is necessary to transport lipids
from one organ to another, and the solvent of all our fluids, including plasma,
is water, we have a potential problem... If the lipids were able to circulate
in their free forms in the bloodstream, it would be the tendency of the lipids
to cluster in lipid droplets (such as when olive oil is dropped in a glass of
water), which would, ultimately, lead to the occlusion of blood vessels.
It is
precisely to avoid this situation that the plasma lipoproteins are synthesized.
As the name implies, the lipoproteins are macromolecular complexes composed of
lipids and proteins and have the function of transporting lipids (the only
exception are fatty acids! ) in the bloodstream, keeping them in a partially
soluble state. Basically, the idea is that these are spherical structures with
an extremely hydrophobic interior (mostly composed of the more nonpolar lipids
- triglycerides and phospholipids) and a polar surface to enable interactions
with water. Thus, in the surface there are the polar groups of the
phospholipids and cholesterol. Therefore, by being able to interact with water,
lipoproteins can be in a partially soluble state, preventing the formation of hydrophobic
lipid droplets that occur to minimize the contacts of lipids with water.
There are
several classes of lipoproteins that are grouped according to their density.
Thus , in order of increasing density, we have the chylomicrons, VLDL, IDL (not
a “true” class of lipoproteins), LDL and HDL. Since the lipids are less dense
than water, the greater the fat content of a lipoprotein, the less its density.
Regarding the size of the different lipoprotein classes, this varies inversely
with the density, that is, the denser lipoproteins are the smaller ones.
Regarding the
proteic part of lipoproteins, their components are called apolipoproteins, or
apoproteins. In biochemistry, the prefix "apo " means
"incomplete" or "alone". Therefore, the concept of
apoprotein applies to the protein part of the lipoprotein in the absence of
lipids. The name of the apoproteins is given as follows: prefix "apo",
a capital letter, and, in some cases, a number that may reflect the order of
discovery or the molecular mass. Examples include the apoE or apoB -100. The
apoproteins play several important roles in lipoproteins that will be addressed
in a future post...
Tuesday, March 18, 2014
Monday, March 17, 2014
Wednesday, March 12, 2014
Sunday, March 9, 2014
Wednesday, March 5, 2014
Hydrogen bond
The
hydrogen bond is also referred to as hydrogen bridge, and, as its name implies,
it involves a hydrogen atom. Indeed, this is a particular case of a
dipole-dipole interaction (an interaction established between polar molecules) that
includes a hydrogen atom, and requires specific conditions to be established.
There are
two requirements that have to occur in order to be established a hydrogen bond.
Therefore, not all polar molecules having hydrogen atoms have the ability to
establish this type of interaction... The first requirement that must be acomplished
is the existence of a very electronegative atom in one of the involved
molecules. When I say "very electronegative" I 'm referring to one of
the 3 most electronegative atoms - oxygen, nitrogen or fluorine. This atom will
function as an "acceptor" of hydrogen, due to the fact that it is
very electronegative, and thus it will have a very high electron density on it,
presenting a partial negative charge. The second condition that needs to occur
is the existence of a hydrogen atom covalently bonded to a very electronegative
atom. In this case, the latter acts as a "donor" of hydrogen, and the
hydrogen will present partial positive charge because it is attached to a very
electronegative atom.
So, what
happens is an electrostatic attraction between opposite partial charges,
settling the hydrogen bridge. In biochemistry, the hydrogen bonds, like the
remaining non-covalent forces, are very important. The best known example
concerns the interaction between complementary nitrogenous bases in DNA.
And now... despite
having already written this in another post , I can not resist telling it again:
;)
Do you know
how an electron commits suicide?
It jumps
from the hydrogen bridge!
Saturday, March 1, 2014
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