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NOTES & SHTUFF!!!!!!

Prokaryotes

Eukaryotes

Average diameter of cell is 0.5 5


m

Cells commonly up to 40 m in
diameter and commonly 1000
10,000 times the volume of the
prokaryotic cells
DNA is not circular and is
contained in a nucleus the
nucleus is surrounded by a double
membrane
DNA is associated with protein,
forming structures called
chromosomes
slightly larger (80S) ribosomes
(about 25nm in diameter) than
those of prokaryotes
ER present, to which ribosomes
may be attached
Many types of cell organelle
present (extensive
compartmentalisation and division
of labour)
some organelles are bound
by a single membrane, e.g.
lysosomes, Golgi apparatus,
vacuoles
some are bound by two
membranes (an envelope),
e.g. nucleus, mitochondrion.
Some have no membrane,
e.g. ribosomes
Cell wall sometimes present e.g. in
plants and fungi strengthening
material is cellulose or lignin in
plants, and chitin (a nitrogencontaining polysaccharide similar
to cellulose) in fungi.

DNA is circular and lies free in the


cytoplasm

DNA is naked

Slightly smaller (70S) ribosomes


(about 20nm in diameter) than
those of eukaryotes
No ER present
very few cell organelles none
surrounded by an envelope of two
membranes

Cell wall present wall is


strengthened with murein, a
peptidoglycan (a polysaccharide
combined with amino acids)

Organelle with internal membranes: Endoplasmic Reticulum (ER),


Lysosomes, Mitochondrion, Golgi Apparatus.
Resolution of the light microscope: 200nm
Magnification of the light microscope: 1500x
Resolution of the electron microscope: 0.5nm
Magnification of the electron microscope:

glucose have their OH pointing down. Whilst glucose have their OH


pointing up.
Starch is a mixture of 2 substances: Amylose & Amylopectin:
o Amylose is made by condensations between glucose molecules,
as shown in Figure 2.4a. In this way a long, unbranching chain of
several thousand 1, 4 linked glucose molecules is built up.
o Amylopectin is also made of many 1, 4 linked glucose
molecules, but the chains are shorer than in amylose, and branch
out to the sides. The branches are formed by 1, 6 linkages.
Starch is never found in animal cells. Instead, a substance with molecules
very like those of amylopectin is used as the storage of carbohydrate. This
is called glycogen.
Glycogen, like amylopectin, is made of chains of 1, 4 linked glucose
with 1, 6 linkages forming branches. Glycogen molecules tend to be even
more branched than amylopectin molecules.
Cellulose is the most abundant organic molecule on the planet. The only
difference between cellulose and startc and glycogen is that cellulose is a
polymer of glucose, not glucose.
In the isomer, the OH group on the carbon atom 1 projects above the
ring. In order to form a glycosidic bond with carbon atom 4, where the OH
group is below the ring, one glucose molecule must be upside down
(rotated 1800) relative to the other. Thus successive glucose units are
linked at 1800 to each other.
Triglycerides are made by the combination of three fatty acid molecules
with one glycerol molecule. Fatty acids are organic molecules which all
have a -COOH group attached to a hydrocarbon tail. Glycerol is a type of
alcohol.
Each of the three fatty acids molecules joins glycerol by a condensation
reaction.
Triglycerides are insoluble in water but are soluble in certain organic
solvents, including ether, chloroform and ethanol.
Triglycerides are non-polar and hydrophobic
Phospholipids are a special type of lipid. Each molecule has the unusual
property of having one end which is soluble in water. This is because of the
three fatty acid molecules is replaces by a phosphate group, which is polar
and can therefore dissolve in water.
Some fatty acids have double bonds between neighbouring carbon atoms.
Such fatty acids are described as unsaturated (as they do not have the
maximum possible amount of hydrogen) and form saturated lipids. Double
bonds make fatty acids and lipids melt more easily.
Animal lipids are often saturated and occur as fats, whereas plant lipids
are often unsaturated and occur as oils.
All Amino Acids have a central carbon atom which is bonded to an amine
group, -NH2, and a carboxylic acid group, -COOH. The third component
which is always bonded to the carbon atom is a hydrogen atom. The only
way in which amino acids differ from each other is in the remaining,
fourth, group of atoms bonded to the central carbon. This is called the R
group.
When 2 amino acids join together one loses a hydroxyl (-OH) group from
its carboxylic acid group, while the other loses a hydrogen atom from its

amine group. This leaves a carbon atom of the first amino acid free to
bond with the nitrogen atom of the second. He link is called a peptide
bond. This is a condensation reaction (forms water). The oxygen and two
hydrogen atoms removed from the amino acids form a water molecule.
A molecule made up of many amino acids linked together by peptide
bonds is called a polypeptide.
In living cells ribosomes are he sites where amino acids are joimed
together to form polypeptides
Polypeptides can be broken down to amino acids by breaking the peptide
bonds. This is a hydrolysis reaction involving the addition of water.
A polypeptide/protein molecule contains 4 structures:
o Primary Structure: A Polypeptide or protein molecule may contain
several hundred amino acids linked into a long chain, and the
sequence in which they are joined, is called the primary structure of
the protein.
o Secondary Structure: The amino acids in a polypeptide chain have
an effect on each other even if they are not directly next to each
other. A polypeptide chain, or part of it, often coils into a corkscrew
shape called an -helix. This is due to hydrogen bonding between
the oxygen of the CO group of one amino acid and the hydrogen of
the NH group of the amino acid four places ahead of it.
Sometimes hydrogen bonding can result in a much looser
straighter shape than the -helix being formed, called a -pleated
sheet.
o Tertiary Structure: The way in which a protein coils up to form a
precise three-dimensional shape is known as its tertiary structure.
There are four types of bonds that help to keep the folded proteins
in its precise shape which are: Hydrogen Bonds, Disulphide bonds,
Ionic bonds & Hydrophobic interactions.
o Quaternary Structure: Many protein molecules are made up of two
or more polypeptide chains in each molecule. The Association of
different polypeptide chains is called the quaternary structure of the
protien. Haemoglobin is an example of this, having four polypeptide
chains in each molecule. The association of different polypeptide
chain is called the quaternary structure of the protein. The chains
are held together by the the same four types of bond as in the
tertiary structure.
Haemoglobin is the oxygen-carrying pigment found in red blood cells, and
is a globular protein. it has a quaternary structure Each chain is itself a
protein known as globin. Globin is related to myoglobin and so has a very
similar tertiary structure. There are many types of globin 2 of which are
used to make haemoglobin which are known as -globin and -globin. The
haemoglobin molecule is nearly spherical. The four polypeptide chains
pack closely together, their hydrophobic R groups pointing towards the
centre of the molecule, and their hydrophilic ones pointing outwards.
Collagen is the most common protein found in animals. It is an insoluble
fibrous protein. A collagen molecule consists of three polypeptide