Genes and health Flashcards
2.3) Explain, with the use of diagrams, how changing the size of an organ or
organism affects the surface area to volume ratio
As an organism increases in size, surface area to volume ratio decreases. Larger organisms have evolved to have a larger surface area to volume ratio in two different
ways. They may be long and thin thereby providing a larger surface area to volume ratio than being spherical or the may have special organs which increase their surface area to volume ratio such as lungs or intestines.
2.4) State the formula for Fick’s Law
Rate of diffusion surface area x difference in concentration
thickness of gas exchange surface
2.8)Describe how Fick’s Law can be used to explain the rapid rate of diffusion in a lung
The rapid rate of diffusion in the lungs occurs because:
A large surface area:
A branched system of tubes
ending in many alveoli.
Many capillaries surrounding
alveoli.
A large difference in concentration (concentration gradient):
Ventilation (breathing in and
out) replaces air that has lost
some oxygen.
Continuous blood flow, replaces oxygenated blood with deoxygenated blood.
A small distance for diffusion to occur over:
Alveolar walls are one cell thick and these cells are thin.
Capillary walls are one cell thick and these cells are thin.
Capillaries are only just wide enough for Red Blood cells to pass through.
2.10)Draw a diagram of an amino acid including the following labels: amino group, carboxylic acid group, R group
2.11)Identify the part of an amino acid molecule which is variable
All amino acids have a amino group.
There are 20 different types of amino acids and each one has a different R-group.
All amino acids have a carboxylic acid group.
2.12)Draw a labelled diagram
demonstrating the condensation and hydrolysis of peptide bonds: include amino acid monomers, dipeptides and polypeptides
The diagram shows a condensation reaction to produce a dipeptide (2 amino acids joined together).
Reversing this reaction – by adding water in to break apart a dipeptide is a hydrolysis reaction.
Adding many amino acids in a chain using multiple condensation reactions produces a polypeptide (a molecule made up of many amino acids).
2.13)Describe what is meant by the “primary structure of a protein”
The “primary structure of a protein” is the number and sequence of amino acids in a polypeptide chain
The amino acids are joined by peptide bonds
2.14) Describe what is meant by the “secondary structure of a protein”, including sketches to show the two different types, and the bonding involved
Secondary structure:
The most common is an extended
spiral spring, the alpha-helix. The helix shape is held by hydrogen bonding only. Most proteins have at least part of their structure in the form of an alpha-helix.
Alternatively, parallel chains may be
held by hydrogen bonds in an
arrangement known as a β-pleated
sheet. Within one protein molecule
there may be sections with α-helices
and β-pleated sheets.
2.15)Describe what is meant by the “tertiary structure of a protein”, including all the possible bonds involved
The “tertiary structure of a protein” is the folding into an overall 3- dimensional shape. The shape is determined by the location of bonds between R-groups of amino acids (and so determined by the primary structure of the polypeptide chain).
The bonds that hold the tertiary structure together are:
* Disulphide bonds (between two R-groups that contain sulphur)
* Ionic bonds (between positively and negatively charged R-groups)
* Hydrogen bonds (between d+ and d- R-groups)
* Hydrophilic / Hydrophobic interactions (water loving tend to be
external part of enzyme and water hating on interior of protein)
2.16) Give an example of a tertiary protein, and explain why denaturation may cause the protein / polypeptide to not work
An example of a tertiary protein is an enzyme.
Denaturing by heat – the kinetic energy causes the hydrogen bonds
in the protein to break, so changing the shape of the active site. The
substrate can no longer bind so no ESCs can be formed. The enzyme
is denatured.
Denaturing by pH – ionic bonds in the protein break, so changing
the shape of the active site. The substrate can no longer bind so no
ESCs can be formed. The enzyme is denatured.
2.17) Describe what is meant by the “quaternary structure of a protein”, including all the possible bonds involved
Quaternary structure
Only found in complex proteins. Two or more polypeptide chains curl together to form the complete protein molecule. The different polypeptide chains are held
together by
Hydrogen bonds – a weak bond, but if it occurs frequently it can add to molecular stability. Easily broken down, by too high temperatures for example.
Ionic bonds – susceptible to changes in pH (e.g. enzyme structure is affected by
changes in pH).
Disulphide bonds – a strong bond between amino acids which have sulphur in their R groups.
Hydrophobic interactions - some R groups are non-polar, and so are arranged so they face the inside of the protein molecules, as they are water-repelling. Water is thus excluded from the centre of the protein molecules.
2.18) Give an example of a quaternary protein, and explain why denaturation may cause the protein to not function
Haemoglobin is a quaternary protein.
During denaturation, the hydrogen bonds break, causing the haemoglobin to lose its 3-d shape.
This means that the oxygen cannot bind and so the haemoglobin cannot transport oxygen.
2.19) Using a diagram describe the structure of the fibrous protein collagen and relate the structure of collagen to its function as a structural protein
Collagen is the most abundant protein in you. It is found in all the connective tissues of the body.
A collagen fibre is made of 3 long parallel polypeptide molecules wound around each other to make a rope-like strand.
Each fibre cross links (hydrogen bonding) with other fibres to produce a molecule with very great strength.
Apart from being very strong, fibrous proteins are insoluble in water and metabolically inactive.
Collagen is mostly made of secondary structure proteins.
2.20) Using a diagram describe the structure of the globular protein
haemoglobin and relate the structure of haemoglobin to its function as an oxygen transport pigment
Quaternary structure
Only found in complex proteins. Two or more polypeptide chains curl together to form the complete protein molecule.
The shape is held by bonds:
* Hydrogen bonds
* Ionic bonds
* Disulphide
* Hydrophobic interactions
Non-amino acid components may be included in the protein molecule of tertiary and quaternary proteins (e.g. haemoglobin has 4 polypeptide chains and 4 haem groups,
containing iron).
These are called prosthetic groups.
Oxygen binds to the haem prosthetic groups.
Water-soluble, metabolically active, mostly made of tertiary and quaternary protein
structure.
2.21) Draw and label a diagram of a phospholipid molecule, including regions which are hydrophobic and hydrophilic
A phospholipid molecule:
A hydrophilic head:
the head is attracted to water and so points out of the membrane (either in contact with the watery tissue fluid or the watery cytoplasm).
Two hydrophobic tails:
The tails are repelled by water and so point into the centre of the membrane (away from the watery tissue fluid or the watery cytoplasm). They form a fatty barrier around the cell.
2.24) Describe and explain the effects of changing temperature on the permeability of cell membranes
Excess heat causes the molecules within the channel / carrier proteins to vibrate (due to increased kinetic energy).
Hydrogen bonds in the proteins break, and the proteins lose their shape.
The proteins now allow molecules to freely pass through them (e.g. the pigment in beetroot cells).
2.25) Describe and explain the effects of changing alcohol concentration the permeability of cell membranes
Alcohols, such as ethanol, dissolve the phospholipid bilayer, so
allowing molecules to freely pass through the membrane.
2.26) Describe a safe, reliable method for measuring the effect of temperature on the permeability of membranes
Use a cork borer to cut 1cm length cylinders of beetroot
1) Rinse the cylinders in distilled water to remove all dye on the surface of the cylinder
2) Place one beetroot cylinder in each of boiling tubes
3) Add 20cm3 of water to each of the 5 boiling tubes
4) Place in thermostatically controlled water baths for 30 mins (0oC,20oC,40oC,60oC,80oC)
5) Swirl a boiling tube to evenly distribute the pigment throughout the liquid
6) Pour some of the liquid into a cuvettte
7) Zero the colorimeter using a cuvette of distilled water
8) Place the cuvette into the colorimeter and measure the % absorbance of the liquid
9) Repeat for all boiling tubes
10)Repeat each temperature 10 times.
2.26) Describe a safe, reliable method for measuring the effect of alcohol concentration on the permeability of membranes
Use a cork borer to cut 1cm length cylinders of beetroot
1) Rinse the cylinders in distilled water to remove all dye on the surface of the cylinder
2) Place one beetroot cylinder in each of 6 boiling tubes
3) Add 20cm3 of the appropriate alcohol to each of the 6 boiling tubes
(distilled water 0%, 20%,40%, 60%, 80%, 100%)
4) Leave for 30mins at room temp 20oC
5) Swirl a boiling tube to evenly distribute the pigment throughout the liquid
6) Pour some of the liquid into a cuvettte
7) Zero the colorimeter using a cuvette of distilled water
8) Place the cuvette into the colorimeter and measure the % absorbance of the liquid
9) Repeat for all boiling tubes
10)Repeat each ethanol concentration 10 times.
2.27)Draw a diagram explaining
how substances can be moved across a membrane by diffusion
Diffusion is the passive, net movement of molecules from a higher concentration to a lower concentration down its concentration gradient.
Small, non-polar molecules (e.g.
oxygen, carbon dioxide, water) can
diffuse through a membrane by passing between the phospholipid molecules.
This is also known as “simple diffusion”.
2.28)Define the term “osmosis”
The passive, net movement of free water molecules across a partially permeable membrane from a high water concentration to a low water concentration down the diffusion gradient.
2.29) Explain how osmosis is different to diffusion
Diffusion is the net movement of liquid or gas molecules or ions
from where they are in a high concentration to where they are in
a lower concentration.
Osmosis is a special form of diffusion involving the movement of water molecules across a partially permeable membrane. It is the net movement of water molecules from a region where the water molecules are at a high concentration to a region where the water molecules are at a lower concentration, through a partially permeable membrane.
2.30)Draw a diagram explaining
how substances can be moved across a membrane by facilitated diffusion, including protein specificity
Facilitated diffusion is the passive, net movement of molecules across a
membrane from a higher concentration to a lower concentration through a channel protein or a carrier protein.
Ions (small, charged) pass through
channel proteins.
Larger polar molecules (e.g. glucose,
amino acids) pass through carrier
proteins by binding to them. The carrier proteins changes shapes to let them through.
Channel and carrier proteins are a
specific shape so they only allow one
type of molecule through.
2.31)Draw a diagram explaining
how substances can be moved across a membrane by active transport including protein specificity
Active transport is the active movement of molecules across a membrane from a lower concentration to a higher concentration through a protein carrier.
Active means the process requires energy in the form of ATP.
Larger or polar molecules (e.g. glucose, amino acids, ions) can pass through membranes in this way.
The molecule attaches to a binding site on the protein in order to be transported. The binding site is a
specific shape so they only allow one type of molecule to attach and so only one type of molecule is
transported through.
The protein carriers are specific to one type of molecule due to their shape.
2.32, 2.33)Draw a diagram explaining how substances can be moved across a membrane by endocytosis and exocytosis
Endocytosis is the active movement of molecules into a cell using vesicles. Molecules are packaged into vesicles formed from an infolding of the cell surface membrane.
Active means the process requires energy in the form of ATP.
Large particles (e.g. bacterial cell in pohagocytosis) can pass through membranes in this way.
Exocytosis is the active movement of molecules out of a cell using vesicles. Molecules are packaged into vesicles
formed by the Golgi apparatus. The vesicle travels to the cell surface membrane and fuses with it, thereby releasing the molecules out of the cell.
Active means the process requires energy in the form of ATP.
Large molecules (e.g. hormones, enzymes) can pass through membranes in this way.