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المحاضرة ٢
المحاضرة ٢
المحاضرة ٢
The aim of the lesson: to form a system of knowledge about the structure and function
of the basic chemical substances included in the cell
SESSION OBJECTIVES:
1. To study the structure and function of water in the cell.
2. To study the structure and function of carbohydrates in the cell.
3. To study the structure and function of lipids in the cell.
4. To study the structure of proteins in the cell.
5. To develop skills definitions on slides various types of inclusions in cells.
SOFTWARE ISSUES:
1. The functions of water in a living organism.
2. Classification, structure and functions of carbohydrates in the cell.
3. The structure and functional role of lipids in the cells and organisms.
4. Structural organization of proteins.
5. The main types of cellular inclusions, their classification and characteristics of localization in
the cell.
Equipment:
1. Microscope "Biolam P-11".
2. Slides and schemes.
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Exercise 1. Structure and function of the water in the cell.
1.1. Read the text.
2. Water has a high specific heat capacity - the approximate value is 4200J/kg°C. This
means that to raise the temperature of 1kg of water by 1°C, 4200J of energy are required, so the
temperature of water is not easily changed. Water has a high specific heat capacity which means
it adsorbs a lot of heat energy for its temperature rise, and loses a lot to cool. This help to:
- reduce temperature fluctations in organisms - especially large ones.
- minimise increases in temperature in cells as a result of biochemical reactions.
- reduce fluctations in temperature in aquatic habitats.
3. Water has a high heat of vaporization (a lot of heat is needed to turn water into
vapour). Because the transition of water from a liquid to a gas requires the input of energy to
break its many hydrogen bonds, the evaporation of water from a surface causes cooling of that
surface. This helps to:
- many organisms dispose of excess body heat by evaporative cooling; for example,
humans and many other vertebrates sweat.
- in plants evaporation of water from leaves has a cooling effect.
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4. Water has a lower density of ice. Water molecules in an ice crystal are spaced
relatively far apart because of hydrogen bonding. Water is denser as a liquid than as a solid:
- cold water forms ice on the upper surface, insulating the aquatic organisms below.
- water must lose a relatively large amount of heat energy to freeze, making the formation
of ice crystals in cells less likely.
5. Water has a high specific tension and water molecules have cohesive forces holding
them together, due to hydrogen bonding between water molecules. This helps to:
- allow aquatic insects to walk on the surface of water.
- water to be pulled through xylem in plants. Transpiration of water from the stomata
allows water to be pulled up the stem. This brings essential nutrients with it.
7. Water is not easily compressed and has an important role in support in plants and
animals. The uptake of water by plant cells creates a pressure against the rigid cell wall. This
turgor pressure helps non-woody plants to remain upright.
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5. The function of mechanical protection. Subcutaneous adipose tissue of animals
protects organs from knocks and bumps.
6. The source function of education:
• endogenous water - water produced within the body as a result of the biochemical
reactions. The camel is the humps in fat. The oxidation of 100 g fat 105 g of water is released.
• sex hormone (testosterone, estrogens, progesterone, etc.);
• fat-soluble vitamins (A, D, E).
7. Grease as a lubricant at the aquatic animals.
Phospholipids are among the most important molecules of the cell, as they form the core
of all biological membranes. An individual phospholipid is a composite molecule, made up of
three kinds of subunits:
1. Glycerol, a three-carbon alcohol, with each carbon bearing a hydroxyl group. Glycerol
forms the back bone of the phospholipid molecule.
2. Fatty acids, long chains of C—H bonds (hydrocarbon chains) ending in a carboxyl (—
COOH) group. Two fatty acids are attached to the glycerol backbone in a phospholipid
molecule.
3. Phosphate group, attached to one end of the glycerol. The charged phosphate group
usually has a charged organic molecule linked to it, such as choline, ethanolamine, or the amino
acid serine. The phospholipid molecule can be thought of as having a polar “head” at one end
(the phosphate group) and two long, very nonpolar “tails” at the other. In water, the non-polar
tails of nearby phospholipids aggregate away from the water, forming two layers of tails pointed
toward each other—a lipid bilayer. Because the C—H bonds in lipids are very nonpolar, they are
not water-soluble, and aggregate together in water. This kind of aggregation by phospholipids
forms biological membranes.
2.2. Draw the structure of phospholipid.
Phospholipid molecules are amphipathic, i.e.
they consist of a polar, hydrophilic (water-
loving) head and a non-polar, hydrophobic
(water-hating) tail. The polar heads are mainly
derived from glycerol conjugated to a
nitrogenous compound such as choline,
ethanolamine or serine via a phosphate bridge
as shown in diagram (b). The phosphate group
is negatively charged whereas the nitrogenous
group is positively charged. The non-polar tail
of the phospholipid molecule consists of two
long-chain fatty acids each covalently linked to
the glycerol component of the polar head.
3.2. Draw the scheme of converting a linear molecule of glucose into the cyclic molecule:
3.3. Draw the structural formula of ribose, deoxyribose, fructose, pyruvic acid:
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There are 4 patterns of
protein:
1. Primary structure –
chain of amino acids connected
by peptide bonds.
The specific amino acid
sequence of a protein is
determined by the nucleotide
sequence of the gene that
encodes the protein.
2. Secondary structure –
helix. The amino acid chain is
twisted in a spiral due to the
formation of hydrogen bonds.
3. Tertiary structure is
globule.
Helix is folded in the
form of globules by:
A) the formation of more
hydrogen bonds.
B) hydrophilic and
hydrophobic interactions
hydrophilic radicals of amino
acids are on the outside of the
globules, hydrophobic radicals of
amino acids are located within
the globule.
C) formation of disulfide
bridges between the radicals of
amino acids that contain sulfur
(cysteine)
D) ionic interactions
Domains. Many proteins
in your body are encoded within
your genes in functional sections
called exons. Each exon-encoded
section of a protein, typically
100 to 200 amino acids long,
folds into a structurally
independent functional unit
called a domain. As the
polypeptide chain folds, the
domains fold into their proper
shape, each more-or-less independent of the others. A single polypeptide chain connects the
domains of a protein. Often the domains of a protein have quite separate functions—one domain
of an enzyme might bind a cofactor, for example, and another the enzyme’s substrate.
4. Quaternary structure – complex of several globules, a combined group of non-
protein atoms. The hemoglobin protein consists of 4 polypeptide chains and gems that contain
iron
1. Deoxyribose
2 3 2. Tymin
4 3. Adenin
4. Phosphate group
1 5. H-bonds
6. Posphodiester
bond
7 8 7. Guanine
5 8. Cytosin