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Prokaryotes
Eukaryotes
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 naked
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