Module 2 – Foundations in biology Flashcards
C2) How do you do gram stain technique
Used to separate bacteria into two groups: Gram-positive bacteria and Gram-negative bacteria
Crystal violet is first applied to a bacteria specimen on a slide, then iodine, which fixes the dye
The slide is washed with alcohol
Gram-positive bacteria retain the crystal violet stain and will appear blue or purple under a microscope
Gram-negative bacteria have thinner cell walls and therefore lose the stain. They are then staying with safranin dye,which is called a counterstain. These bacteria will then appear red
Gram-positive bacteria are susceptible to the antibiotic penicillin, which inhabits the formation of the cell walls
Gram-negative bacteria have much thinner cell walls is not susceptible to antibiotic pencilling
C2) How do you do the acid-fast technique
Are used to differentiate between species of mycobacterium from other bacteria.
A liquid solution is used to carry carbolfuchsin dye into the cells being studied
The cells are washed with a die loot acid solution.
Mycobacteria are not affected by the I said alcohol and retain the stain- bright red
Are the bacteria lose the stain and are exposed to a methylene blue stain, which is blue
C2) What are the features of a light microscope
1) expense
2) Radiation used
3) Size
4) Maximum magnification
5) Maximum resolution
6) Type of image produced
7) sample preparation
8) Vacuum needed?
1) not expensive
2) Light
3) Small and portable
4) x 1500
5) 200 nm
6) 2d
7) Sample procedure
8) No-can you live in specimen
C2) What are the features of a scanning electron microscope
1) expense
2) Radiation used
3) Size
4) Maximum magnification
5) Maximum resolution
6) Type of image produced
7) Vacuum needed?
1) Expensive to buy and operate
2) Beam of electrons
3) Large
4) X 500,000
5) 2.2 nm
6) 3D
7) Yes-dead
C2) What are the features of a transmission electron microscope
1) expense
2) Radiation used
3) Size
4) Maximum magnification
5) Maximum resolution
6) Type of image produced
7) Vacuum needed?
1) Expensive to buy and operate
2) Beam of electrons
3) Large
4) X 1,000,000
5) 0.1 nm
6) 2D
7) Yes-dead
C2) What other parts of an animal cell
Cell-surface membrane
Cytosol
Ribosome
Centriole
Rough endoplasmic reticulin
Smooth endoplasmic reticulin am
Cytoskeleton
Secretion vesicles
Mitochondria
Golgi apparatus
Nucleus
Nucleolus
Golgi Vesicles
Microtubule network
C2) What are the parts of an plant cell
Cell membrane
Cell wall
Ribosome
Rough endoplasmic reticulin
Smooth endoplasmic reticulin
Mitochondria
Golgi apparatus
Nucleus
Nucleolus
Golgi Vesicles
Chloroplast
Vacuole membrane
Raphide crystal
Druse Crystal
cytoplasm
Large central vacuole
Amyloplast (starch grain)
C2) What are the structural components of cytoskeleton of a cell
MICROFILAMENTS – Fibres made from the protein Actin. They are responsible for movement of the cell and cytoplasm during Cytokinesis.
MICROTUBULES – Formed by the globular protein Tubulin. They polymerise to form tubes that determine the shape of the
cell. They also act as tracks for organelles moving around the cell.
INTERMEDIATE FIBRES – Gives strength to
cells and helps maintain integrity.
C2) What is the function of the cytoskeleton of a cell
Providing mechanical strength to cells
Aiding transport within cells
Enabling cell movement.
C2) What are the structural components of the nucleus of a cell
Double Nuclear Envelope – A double membrane which
compartmentalises the Nucleus and prevents damage. Protects the DNA.
Nuclear Pores – Allows molecules to enter and leave the cell
Nucleolus – Site of ribosome production. Composed of RNA and
proteins.
Chromatin – is the DNA. Contains the Genetic Code which controls the activity of the cell.
C2) What is the function of the nucleus of a cell
1) Controls all the activity of the cell.
2) Where the Genetic Code (DNA) of the cell is stored, replicated, and copied into RNA (transcribed).
The Nucleus is attached to the Rough ER so the mRNA can easily get to ribosomes.
C2) What are the structural components of the Rough Endoplasmic Reticulum of a cell
System of hollow tubes and
membrane bound sacs which form sheets called cisternae.
attached to the nucleus and covered with ribosomes.
Consists of an interconnected system of
flattened sacs.
C2) What is the function of the Rough Endoplasmic Reticulum of a cell
Site of protein synthesis.
C2) What are the structural components of the smooth Endoplasmic Reticulum of a cell
similar to RER but lacks ribosomes -is a system of interconnected tubules.
C2) What is the function of the smooth Endoplasmic Reticulum of a cell
responsible for carbohydrate & lipid synthesis, and storage.
C2) What are the structural components of the ribosome of a cell
A 2 subunit organelle.
Made from RNA and protein.
Not membrane bound.
Very small organelles: about 22nm in diameter.
Found free floating in the cytoplasm or attached to the Rough ER
C2) What is the function of the ribosome of a cell
These are where protein is made.
They assemble amino acids into proteins in chains using mRNA.
C2) What are the structural components of the mitochondria of a cell
Oval shaped.
Surrounded by two membranes (double membrane).
The inner membrane forms finger-like structure called cristae which increases the surface area.
The solution inside is called a matrix which contains enzymes for respiration.
Mitochondrial DNA – Small amounts of DNA, enable mitochondrion to reproduce and create enzymes.
C2) What is the function of the mitochondria of a cell
Site of aerobic respiration.
As a result of respiration, they produce ATP (energy carrier in cells).
C2) What are the structural components of the Golgi apparatus of a cell
Stack of flattened, membrane bound sacs (cisternae).
These are continuously formed from the ER at one end and budding off as Golgi vesicles at the other.
C2) What is the function of the Golgi apparatus of a cell
Allows internal transport.
Receives proteins from the RER
Modifies and processes molecules (such as new lipids and proteins) and packages them into vesicles.
These may be Secretion vesicles (if the proteins need to leave the cell) or lysosomes (which stay in the cell).
Makes lysosomes
Lipid synthesis
C2) What are the structural components of the lysosome of a cell
They are spherical sacs surrounded by a
single membrane.
C2) What is the function of the lysosome of a cell
They contain powerful hydrolytic
digestive enzymes known as lysozymes.
Their role is to break down worn out components of the cell or digest invading cells.
C2) What are the structural components of the cilia of a cell
‘Hair like’ extensions that protrude from some animal cell types.
In cross section they have an outer membrane and a ring of nine pairs of protein microtubules inside with two microtubules in the middle.
Known as a 9 +2 arrangement.
Arrangement allows movement.
C2) What is the function of the cilia of a cell
sensory function (e.g. nose), beat creating a current to move fluid/mucous/objects
For locomotion
C2) What are the structural components of the flagellum of a cell
Similar to cilia but longer.
They stick out from the cell surface and are surrounded by the plasma membrane.
Like cilia they have a 9 +2 arrangement.
C2) What is the function of the flagellum of a cell
(Whip-like) enables a cells mobility.
The microtubules contract to make the flagellum move.
Propel cells forward e.g. sperm cells.
C2) What are the structural components of the chloroplast of a cell
Double membrane which encloses the
stroma.
Stroma contains: Starch grains, lipid stores, DNA, RNA, ribosomes.
Series of membrane-bound flattened sacs called thylakoids in the stroma.
Thylakoids stacked together are called grana.
Grana are linked together by lamellae.
The grana contain chlorophyll
C2) What is the function of the chloroplast of a cell
Photosynthetic reactions
C2) What are the structural components of the Large Permanent Vacuole of a cell
Single membrane bound (membrane is called a tonoplast).
Contains a fluid called cell sap (solution of mineral salts, sugars, amino acids, wastes etc).
Selectively permeable barrier
C2) What is the function of the Large Permanent Vacuole of a cell
Stores cell cap
Support herbaceous plants by making cells turgid.
Helps maintain shape and gives support by maintaining turgor pressure.
Sugars and amino acids act as a temporary food store.
C2) What does the DNA look like in a prokaryotic cell
The structure of DNA is fundamentally the same as in eukaryotic cells but it is packed differently
Prokaryote generally only have one molecule of DNA, A chromosome, which is supercoiled to make it more compact.
The genes on the chromosomes are often grouped into operons, meaning a number of jeans are switched on or off at the same time
C2) What does the ribosomes look like in a prokaryotic cell
Are smaller than those in eukaryotic cells.
The relative size is determined by the rate of which they settle, or form a sediment in solution.
The larger eukaryotic ribosomes are designed 80s in the smaller prokaryotic ribosomes are 80s
Both are necessary for protein synthesis, although the larger 80s ribosomes are involved in the formation of more complex proteins
C2) What does the cell wall look like in a prokaryotic cell
Made from peptidoglycan, also known as murein
A complex polymer formed from amino acids and sugars
C2) What does the flagella look like in a prokaryotic cell
The flagella of prokaryotes is thinner than the equivalent structure of eukaryotes and does not have the 9+2 arrangement
The energy needed to move the flagellum is supplied by the process of chemiosmosis, not from ATP as in eukaryotic cells
C2) What are the features of a Eukaryotic cell
1) Nucleus
2) DNA
3) DNA orientation
4) Extra chromosomal DNA
5) Organelles
6) Cell wall
7) Ribosomes
8) Cytoskeleton
9) Reproduction
10) Cell type
11) Cell-surface membrane
1) Present
2) linear
3) Associated with proteins called histones
4) Only present in the certain organelles such as chloroplasts and mitochondria
5) Both membrane-bound and non-membrane-bound
6) Chitin in fungi, Celulose in plants, not present in animals
7) Larger, 80s
8) Present, more complex
9) asexual or sexual
10) Unicellular and multicellular
11) Present
C2) What are the features of a prokaryotic cell
1) Nucleus
2) DNA
3) DNA orientation
4) Extra chromosomal DNA
5) Organelles
6) Cell wall
7) Ribosomes
8) Cytoskeleton
9) Reproduction
10) Cell type
11) Cell-surface membrane
1) Not present
2) Circular
3) Proteins fold and condense DNA
4) Circular DNA called plasmids
5) Non membrane-bound
6) Peptidoglycan
7) Smaller, 70s
8) Present
9) Binary fusion
10) Unicellular
11) Present
C4) why are enzymes important
So that chemical reactions can happen very fact
Enzymes are biological catalysts
They are globular proteins that interact with substrate molecules
C4) What is the role of enzymes in a reaction?
Involves in the synthesis of large polymer-based components
Digestion is also catalysed by range of enzymes
C4) How does an enzyme action work?
For a reaction to happen molecules need to collide in the right orientation. When High temperatures and pressure are applied the speed of the molecules will increase, so will the number of successful collisions and the overall rate of reaction
Different enzymes are produced by living organisms as each enzyme catalyses one biochemical reaction of which there are thousands in every given cell. This is termed the specificity of the enzyme
Energy needs to be supplied for most reactions to start this is called activation energy.
C4) What is the meaning of anabolic reactions
The chemical reactions required for growth are anabolic (building up) reactions and they are all catalysed by enzymes
C4) what is the meaning catabolic reactions.
Energy is released from large organic molecules like glucose, in metabolic pathways consisting of many catabolic (barking down) reactions. Catabolic reactions are also catalysed by enzymes
C4) What is the meaning of Metabolism
Reactions rarely happen in isolation but as part of a multi-step pathways. Metabolism is the sum of all the different reactions and reaction pathways. Can only happen because of the control and order imposed by enzymes .
C4) What is Vmax
Enzymes can only increase the rate of a reaction to a certain point
C4)How does an enzyme affect the activation energy of a reaction
The amount of energy needed is so large it prevents a reaction in happening. Enzymes help the molecules collide successfully and therefore reduce the activation energy required
C4) What is the lock and key hypothesis
In the same way that only the right key will fit into a lock only a specific substrate will fit the active site of an enzyme
When the substrate is bonded to the active site and enzyme substrate complex is formed.
The substrate that reacts and the product are formed in a enzyme product complex
C4) what is the active site
An area within the tertiary structure of the enzyme, that has a shape complimentary to the shape of a specific substrate molecule
C4) how is the substrate broken down in the active site.
The substrate is held in away by the enzyme that the right atom groups are close enough to react. the R-groups within the active site of the enzyme will also interact with the substrate, forming temporary bonds. This puts strain on the bonds within the substrate helping the reaction to occur
C4) What is the induced fit hypothesis of an enzyme
Research suggests that the active site of the enzyme actually changes shape slightly as the substrate enters.
This is a modification on the lock and key hypothesis.
The initial interaction between the enzyme and substrate is relatively weak but these week interactions rapidly changes the enzymes Tertiary structure that strengthen binding, putting strain on the substrate molecule. This can weaken a particular bond in the substrate therefore lowering the activation energy for the reaction
C4) What are intracellular enzymes
Enzymes that work within a cell
C4) How does an intracellular enzyme help
The synthesis of polymers from monomers. For example polysaccharides from glucose require enzymes
An example of this is hydrogen peroxide
C4) what are extracellular enzymes
All of the reactions happening within cells need substrates to make the product. The substrate need to be constantly supplied to cells. Nutrients present in the diet or environment of the organism supply these substrates
Nutrients are supplied in the form of polymers such as proteins and polysaccharides. These large molecules can’t enter cells directly. They need to be broken down
Enzymes are released from cells to break down these large nutrient molecules into smaller molecules in the process of digestions. These are called extracellular enzyme they work outside the cell that made them.
C4) How is starch digested
It begins in the mouth and continues in the small intestine
1) Starch polymers are broken down into maltose a disaccharide. The enzyme involved is called amylase produced by the saliva glands and the pancreas. Released in the saliva into the mouth and in pancreatic juice into the small intestines
2) maltose is broken down into glucose which is a monosaturated using the enzyme maltase which is present on the small intestine
C4) how is protein digested
Trypsin is a protease enzyme that catalyse proteins into smaller peptides which can then be broken down into amino acids.
Trypsin is produced in the pancreas and released with the pancreatic juice into the small in testing and acts on proteins.
C4) how can an enzyme structure be affected
By factors such as temperature and pH. They cause a change in the shape of the active site.
C4) how does temperature affect the rate of a reaction of an enzyme
Increasing the temperature, increases the kinetic energy of the particles. As temperature increases the particles move faster and collide more frequently.
Increasing the temperature will result in more frequent successful collisions between substrate and enzyme leading to an increase in the rate of reaction
C4) What is the definition of the temperature coefficient of the reaction
In enzyme
Is a measure of how much the rate of a reaction increases with a 10°C rise in temperature
For an enzyme reaction it is usually two meaning that the rate of reaction doubles with a 10°C temperature increase
C4) how does enzymes denature from temperature
As enzymes are proteins high temperatures affect the bonds holding the protein together making it vibrate more.
As the temperature increases the vibration increases onto the bonds strain and then break
The breaking of these bonds result in changes in the tertiary structure of the protein
Meaning it has denatured
When an enzyme is denatured the shape of the active site has changed and no longer complimentary to substrate therefore enzyme Will not function as a catalyst
C4) what is the optimal temperature of an enzyme
Optimal temperature is the temperature at which enzymes have the highest rate of activity.
In the human body optimum temperature is around 40°C
In thermophilic bacteria (Hot Springs) the optimal temperature is around 70°C
In psychrophilic organisms (cold areas) the optimal temperature is below 5°C
C4) how does denaturing above and below the optimal temperature affect the rate of a reaction
Denaturing above the optimal temperature, decreases the rate of reaction rapidly. This is because all of the enzyme molecules have a change in the active site and and it happens at about the same temperature so the loss of activity is rapid
Denaturing below the optimal temperature, decreases The rate of reaction. This is because the enzyme has not denatured they are just less active
C4) how do enzymes adapt to extremely cold environment
They tend to be more flexible structures, particularly that the active site making them less stable than enzymes to work at higher temperatures. Smaller temperature changes will denatured them
C4) how to enzymes adapt to extremely hot environments
The enzymes in these organisms are more stable than enzymes in other organisms this is due to the increased number of bonds, particularly hydrogen bonds and sulfer bridges in the tertiary structure.
The shapes of these enzymes and the active site are more resistant to change as the temperature rises
C4) how does PH affect an enzyme reaction
As enzymes are proteins, the hydrogen bonds and ionic bonds between amino acid r groups hold proteins in the precise 3-D shape because of interactions between polar R groups
The change in pH refers to a change in the hydrogen ion concentration. More hydrogen ions present in the low pH environment. Fewer hydrogen ions present in high pH environments
Hydrogen ions interact with polar r groups therefore increasing hydrogen ions increases the interactions. So more hydrogen ions present the less r groups are able to interact with each other this leads to bonds breaking and shapes changing. Reverse for lower PH
The active site will be at the right shape at a certain hydrogen ion concentration known as the optimal PH
When the pH changes The structure of the enzyme and therefore the active site is altered
C4) what is a renaturation of an enzyme
If the pH returns to the optimal then the protein will resume its normal shape and catalyse the reaction again
C4) How does an increased Number of substrate molecule affect the rate of a reaction
Leads to a higher collision rate with the active site of the enzyme and formation of a more enzyme substrate complexes therefore an increased rate of reaction
c4) how does an increased number of enzyme concentration affect the rate of a reaction
Will increase the number of available active sites in a particular area leading to an increase in enzymes from free complexes at a faster rate therefore increase the rate of a reaction
C4) what happens when the rate of reaction increases to V-max
At this point all of the active site occupied by substrate particles and no more enzyme substrate complex is can be formed into products are released from the active site
C4) what is an enzyme inhibitor
What are the two types of enzyme inhibitors
Inhibitors are molecules that prevent enzymes from carrying out the normal function of catalystis
Competitive and non-competitive enzyme inhibitors
C4) How does competitive inhibitor affect the rate of a reaction
Competitive inhibitors reduce the rate of reaction from a given concentration of substrate but does not change the Vmax of the enzyme it inhibits
If Substrate concentration is increased enough there will be so much more substrate than inhibitors that the original Vmax can still be reached
C4) how does it and non-competitive inhibition work
The inhibitor binds to the enzyme at a location other than the active site this is called an allosteric site
The binding of the inhibitor causes the tertiary structure of the enzyme to change meaning the active site changes shape
This results in the active site no longer being complimentary shape to the substrate so unable to bind to the enzyme
The enzyme cannot carry out its function and is inhibited
C4) What are examples of irreversible noncompetitive inhibitors
Irreversible inhibitors cannot be removed from the part of the enzyme they are attached to. They are often very toxic but not always.
Protein pump inhibitors are used to treat long-term indigestion. They Irreversibly block and enzyme system responsible for secreting hydrogen ions into the stomach
C4) why is end product inhibition important
A control mechanism for the reaction.
Excess products are not made and resources are not wasted.
It is an example of non-competitive reversible inhibition
C4) what are cofactors and co-enzymes
Some enzymes need a non-protein helper component in order to carry out the function as biological catalysts
They may transfer atoms or groups from one reaction to another in a multistep pathway or may actually form part of the active site of an enzyme this component is called a cofactor
If the cofactor is an organic molecule it is called a coenzyme
C4) how are coenzymes obtained
They are derived from vitamins, a class of organic molecules found in the diet.
For example vitamin B5 which is used to make coenzyme A essential in the breaking down of fatty acids and carbohydrates in respiration
C4) what is precursor activation
Many enzymes are produced in an inactive form known as inactive precursor enzymes
Particular enzymes can cause damage within the cell producing them water tissues where they are released, or enzyme this action needs to be controlled and only activated under certain conditions
C4) how are precursor enzyme activated
Precursor enzymes often need to undergo change in the tertiary structure particularly to the active site.
This can be achieved by the addition of a cofactor.
Before the cofactors added the precursor protein is called an apoenzyme. When the cofactors and in the enzyme is activated it is called a holoenzyme
Sometimes the change is brought about by the action of another enzyme. Sometimes a change in conditions such as pH or temperature and bring about the change these types are called proenzymes
C4) what is the prosthetic group
They are cofactors, required by certain enzymes to carry out the catalytic function.
Whilst some cofactors are loosely or temporarily bonded to the enzyme protein in order to activate them.
Prosthetic group are tightly bound and form a permanent feature of the protein
C4) how are inorganic cofactors obtained
Obtained via the diet and minerals including iron, calcium, chloride and zinc ions.
For example the enzyme amylase which breaks down starch is contain a chloride ions, necessary for the formation of a correctly shaped Active site
C4) how does competitive inhibition work
A molecule or part of a molecule with a similar shape to the substrate can fit into the active site of an enzyme
This blocks the substrate from entering the active site preventing the enzyme from catalysing the reaction
The ends and cannot carry out its functions and is inhibited
The non-substrate molecule that binds to the active site is a type of inhibitor. Substrate and inhibitor molecule present in a solution will compete with each other to buy into the active site of the enzyme. This will reduce the number of substrate molecules binding to active site in a given time and slow down the rate of a reaction. The degree of inhibition will depend on the relative concentration of substrate, inhibitor and enzyme
Most competitive inhibitor only bind temporarily to the active site, so it is reversible. An exception is aspirin
C4) what are examples of competitor inhibitors
Statins are competitive inhibitor is of an enzyme use in the synthesis of cholesterol. Statins are regularly prescribed to help reduce blood cholesterol concentration which can result in heart disease
Aspirin irreversibly inhibits the active site of COX enzymes
C4) What are the effects of non-competitive inhibitors on the rate of reaction
Increasing the concentration of enzymes or substrate will not overcome the effects of non-competitive inhibitors.
Increasing the concentration of inhibitors how old will decrease the rate of a reaction further as more active sites become unavailable
C4) what is the meaning of end product inhibtion
Term used for enzyme inhibition that occurs when the product of the reaction X as a inhibitor to the enzyme that produces it – Negative feedback
C4) what is the temperature coefficient
R1 / R2
C4) what is an example for cofactors and prosthetic group
Cl – as a cofactor for amylase
Zn2+ as a prosthetic group for carbonic anhydrase a
C5)What are Intrinsic proteins
Are transmembrane protein that are in bedded in both layers of the membrane
Have amino acids with hydrophobic r groups on the external surface which interact with the hydrophobic core of the membrane keeping them in place
C5) what are the two intrinsic proteins and how are they held in position
Channel proteins provide a hydrophobic channel that allows passive movement down a concentration gradient. Held in position by interactions between the hydrophobic core of the membrane and hydrophilic or groups on the outside of the protein
Carrier proteins plays a role in both passive, down a concentration gradient and active transport, against a concentration gradient by changing the proteins shape
C5) What are the uses of glycoproteins within the cell surface membrane
Intrinsic proteins that are embedded in the cell surface membrane with attach carbohydrate chains
Plays a role in Cell adhesion cells joining together to form a tight junction and as receptors for chemical signals
Helps with cell signalling-when the chemical binds to the receptor the cell responds causing a direct response (neurotransmitters at a synaptic junction) or a cascade of events (hormones)
C5) what is the plasma membrane
The cell-surface membrane which separates the cells from its external environment
C5) what is the importance of glycolipids on the cell surface membrane
They are lipids with attached carbohydrate chains
These molecules are called antigens and can you be recognised by the cells of the immune system as self and nonself
C5) what extrinsic proteins
Are present in one side of the bilayer
Normally have hydrophobic r group on the outer surface and interact with the polar heads of the phospholipid bilayer
Can we present in either layer and some moves between layers
C5) What is the importance of cholesterol in the cell surface membrane
Cholesterol is a lipid with a hydrophobic end and a hydrophilic end
Regulate the fluidity of the membrane
Cholesterol molecules positioned between phospholipids in a membrane bilayer
The hydrophilic end interacting with the heads and the hydrophobic end interacting with the tails pulling them together. Therefore adding stability to the membranes without making them rigid
The cholesterol molecule prevents the membrane becoming too solid by stopping the phospholipid molecules grouping too closely and crystallising
C5) How can the cell-surface membrane be a site for chemical reactions
Proteins in the membrane forming organelles or present within organelles have to be in particular positions for chemical reactions to take place
C5) how does temperature affect the permeability of the cell surface membrane
Phospholipids are constantly moving within the membrane when the temperature increases the phospholipid gain more kinetic energy and will move more
Making the membrane more fluid leading to it losing its structure. Continued temperature increase will entirely break down the cell
The loss of structure increases the permeability of the membrane making it easier for particles to cross
Carrier and channel proteins in the membrane will denature at higher temperatures, which is involved in transport across the membrane
C5) Why do solvent affect the permeability of the plasma membrane
Water is essential in the formation of the phospholipid bilayer. The hydrophobic tail of a phospholipid is oriented away from water creating a hydrophobic core and the hydrophilic heads interact with water keeping the bilayer intact
Many organic solvents are less polar or more polar than water which will dissolve membranes and disrupt cells. This is why alcohol is used as an antiseptic wipe as it dissolves the membranes of bacteria in a wound
Pure or very strong alcohol are toxic as they destroy cells. Non-polar alcohol molecules can enter the cell membrane and
the presence of these molecules between the phospholipids disrupt the membrane
When the membrane is disrupted it becomes more fluid and more permeable.
Some cells need intact cell membranes for specific functions for example transmission of a nerve impulse by Neurons, when its membrane is disrupted the nerve impulse no longer transmits as normal for example the changes in peoples behaviour when on alcohol
C5) Why are membranes considered to be partially permeable
Diffusion can only happen if the membrane is permeable to the particle for nonpolar molecules such as oxygen defuses through freely down a concentration gradient
The hydrophobic interior of the membrane repels substances with a positive or negative charge so they cannot pass through.
Polar molecules such as water can diffuse through but at a very slow rate. Smaller polar molecules pass through easier the larger ones
C5) what is facilitated diffusion
When polar molecules pass through a channel protein to diffuse across the membrane
Movement of molecules is down a chemical gradient and does not require external energy
The rate of facilitated diffusion is dependent on temperature, concentration gradient, membrane surface area and thickness but is also affected by the number of channel proteins present