Biology-Nature and variety of living organisms

Characteristics of living organisms

understand how living organisms share the following characteristics:
• they require nutrition
• they respire
• they excrete their waste
• they respond to their surroundings
• they move
• they control their internal conditions
• they reproduce
• they grow and develop.
• Movement: an action by an organism or part of an organism causing a change of position or place.
• Respiration: the chemical reactions that break down nutrient molecules in living cells to release energy.
• Sensitivity: the ability to detect or sense changes (stimuli) in their surroundings and to make appropriate responses.
• Homeostasis:  the ability to control their internal conditions.
• Growth and development: a permanent increase in size and dry mass (growth) and an increase in complexity
(development).
• Reproduction: the processes that make more of the same kind of organism.
• Excretion: the removal from organisms of toxic materials and the waste products of metabolism.
• Nutrition: the taking in of materials for energy, growth and development.

Variety of living organisms

describe the common features shown by eukaryotic organisms: plants, animals, fungi and protoctists
• Eukaryotes are organisms that have a membrane-bound nucleus and organelles inside their cells. 
• They can be unicellular (only one cell) or multicellular (more than one cell).
PLANTS
• Eg: herbaceous legumes (peas), cereals (wheat)
• Multicellular
• Cells contain a nucleus, chloroplasts and cellulose cell walls
• All feed by photosynthesis
• Store carbohydrates as starch or sucrose
• Contain a large, central cell vacuole

ANIMALS
• Eg: humans (mammals), butterflies (insects)
• Multicellular
• Cells contain a nucleus but no cell walls or chloroplasts
• Feed on organic substances made by other living things
• Store carbohydrates as glycogen

FUNGI
• E.g. moulds, mushrooms, yeast
• Most are multicellular with a mycelium of thread-like structures called hyphae which have many nuclei but
some are single-celled (eg yeast is single celled)
• Cells have nuclei and cell walls made from chitin 
• Feed by saprotrophic (on dead or decaying material) or parasitic (on live material) nutrition by
secreting extracellular enzymes onto the food
• May store carbohydrates as glycogen

PROTOCTISTS
• E.g. Amoeba (like an animal), Chlorella (like a plant)
• Most are unicellular 
• All have a nucleus; some may have cell walls and chloroplasts, meaning some protoctists
photosynthesise like plants and some feed on organic substances made by other living things
like animals.
 describe the common features shown by prokaryotic organisms such as bacteria
• Prokaryotes do not have a membrane-bound nucleus or membrane-bound organelles inside their
cells.
• E.g. bacteria (Lactobacillus d. bulgaricus (rod-shaped bacterium used in yoghurt production),
Pneumococcus (spherical bacterium that causes pneumonia). 
• Unicellular and microscopic.
• Have a cell wall, cell membrane, cytoplasm and plasmids.
• Some can carry out photosynthesis but they mainly feed off other organisms, either dead or alive

understand the term pathogen and know that pathogens may include fungi, bacteria, protoctists or viruses
• An organism that causes disease
• Fungi, protoctists, bacteria and viruses can all be pathogens
VIRUSES
• E.g. Tobacco Mosaic Virus, Influenza virus
• Much smaller than bacteria 
• They are not made from cells and are not considered living organisms as they do not carry out all
the life processes
• Parasitic – reproduce inside host cells by hijacking the cell’s mechanisms to make multiple copies
and then bursts out of the cell to spread throughout the host
• Able to infect every type of living cell
• The envelope is used to gain entry into host cells
• The capsid is a protein coat used to protect the genetic information
• The DNA or RNA contains the code for building new viruses

Structures and functions in living organisms

Level of organisation
describe the levels of organisation in organisms:
organelles, cells, tissues, organs and systems
 Cell structure
describe cell structures, including the nucleus, cytoplasm, cell membrane, cell wall, mitochondria, chloroplasts, ribosomes and vacuole
• Cytoplasm is found inside the cell and contains all the other cell structures
• The large nucleus is surrounded by a nuclear membrane to separate it from the cytoplasm
• The cell membrane surrounds the cell
• The cell wall is made of cellulose and surrounds the cell membrane in plant cells
• Mitochondria (singular: mitochondrion) are organelles found throughout the cytoplasm
• Chloroplasts are organelles found in the cytoplasm that are packed with the pigment
chlorophyll and so are green in colour
• Ribosomes are tiny structures that can be free within the cytoplasm or attached to a system of
membranes inside the cell
• Vacuoles are large vesicles that take up a large part of the interior of plant
cell

describe the functions of the nucleus, cytoplasm, cell membrane, cell wall,
mitochondria, chloroplasts, ribosomes and vacuole

know the similarities and differences in the structure of plant and animal cells
 Biological molecules
identify the chemical elements present in carbohydrates, proteins and
lipids (fats and oils)
• Most of the molecules in living organisms fall into three categories:
carbohydrates, proteins and lipids
• These all contain carbon and so are described as organic molecules

describe the structure of carbohydrates, proteins and lipids as large molecules made up from smaller basic units: starch and glycogen
from simple sugars, protein from amino acids, and lipid from fatty acids and glycerol

Carbohydrates
• Long chains of simple sugars
• Glucose  is a simple sugar ( a monosaccharide)
• When 2 glucose molecules join together maltose is formed (a disaccharide)
• When lots of glucose molecules join together starch or glycogen is formed (a polysaccharide)

Proteins
• Long chains of amino acids
• There are about 20 different amino acids
• They all contain the same basic structure but the ‘R’ group is different for each one
• When amino acids are joined together a protein is formed
• The amino acids can be arranged in any order, resulting in hundreds of thousands of different proteins
• Even a small difference in the order of the amino acids results in a different protein being formed

Lipids
• Most lipids in the body are made up of triglycerides
• Their basic unit is 1 fatty acid and 3 glycerols
• The fatty acids vary in size and structure
• Lipids are divided into fats (solids at room temperature) and oils (liquids at room temperature)
 Practical: investigate food samples for the presence of glucose, starch, protein and fat

Test for Glucose

• Add Benedict’s solution into sample solution in test tube
• Heat at 60 – 70 °c in water bath for 5 minutes
• Take test tube out of water bath and observe the colour
• A positive test will show a colour change from blue to orange or brick red

Test for Starch

• Add drops of iodine solution to the food sample
◦ A positive test will show a colour change from brown to blue-black

Test for Protein

• Add drops of Biuret solution to the food sample
• A positive test will show a colour change from blue to violet / purple

Test for Lipid

• Food sample is mixed with 2cm3 of ethanol and shaken
• The ethanol is added to an equal volume of cold water
• A positive test will show a cloudy emulsion forming
 understand the role of enzymes as biological catalysts in metabolic reactions

• Are proteins
• Are biological catalysts (biological because they are made in living cells, catalysts because they speed
up the rate of chemical reactions)
• Are specific to one particular substrate as the active site of the enzyme, where the substrate attaches, is a
complementary shape to the substrate – known as the lock and key hypothesis
• Are affected by changes in temperature and pH
• Are not used up in the reaction they catalyse

understand how temperature changes can affect enzyme function, including changes to the shape of active site
• Enzymes are proteins and have a specific shape, held in place by bonds. This is extremely important around the active site area
as the specific shape is what ensures the substrate will fit into the active site and
enable the reaction to proceed. 
• Enzymes work fastest at their ‘optimum temperature’ – in the human body, the
optimum temperature is 37⁰C.
• Heating to high temperatures (beyond the optimum) will break the bonds that
hold the enzyme together and it will lose its shape. This is known as
denaturation. Substrates cannot fit into denatured enzymes as the shape of
their active site has been lost. 
• Denaturation is irreversible – once enzymes are denatured they cannot regain
their proper shape and activity will stop.
• Increasing the temperature from 0⁰C to the optimum increases the activity of
enzymes as the more energy the molecules have the faster they move and the
number of collisions with the substrate molecules increases, leading to a faster rate of reaction. 
• This means that low temperatures do not denature enzymes, they just make them work more slowly.

practical: investigate how enzyme activity can be affected by changes in temperature

• Starch solution is heated to a set temperature
• Iodine is added to wells of a spotting tile
• Amylase is added to the starch solution and mixed well
• Every minute, droplets of solution are added to a new well of iodine solution
• This is continued until the iodine stops turning blue-black (this means there is no more starch left in the
solution as the amylase has broken it all down)
• Time taken for the reaction to be completed is recorded
• Experiment is repeated at different temperatures
• The quicker the reaction is completed, the faster the enzyme is working

understand how enzyme function can be affected by changes in pH altering the active
site
• The optimum pH for most enzymes is 7 but some that are produced in acidic conditions, such as the
stomach, have a lower optimum pH (pH 2) and some that are produced in alkaline conditions, such as
the duodenum, have a higher optimum pH (pH 8 or 9)
• If the pH is too high or too low, the bonds that hold the amino acid chain together to make up the protein
can be destroyed
• This will change the shape of the active site, so the substrate can no longer fit in
• The enzyme will denature and activity will stop