Gas Exchange

Alveoli is the site of the gas change

Oxygen diffuses into the blood, from alveoli as C2O, which diffuses into alveoli from the
blood

3 things affect the rate of diffusion which are:

1. Concentration gradient
2. Surface Area
3. Thickness of gas exchange service

Rapid gas exchange as they have surface area and they have numerous capillaries around
them together together with ventilation they between alveoli and the air so diffusion is rapid

Cf On Gas Exchange

 Maintain a steep concentration. Short distance

 Very dry sticky mucus on the bronchioles, and the consequences
 Repeated lung infections as bacteria trapped in the dry mucus
 Causes shortness of breath, because mucus blocks in the narrow airways which
prevents air getting to the and from the alveoli below the blockage.
 Causes loss of elasticity in lungs

surface area x difference in

concentration

Rate of diffusion 

thickness of the gas exchange surface

Phospholipid Bilayer
 2 fatty acid tails, and phosphate head.
 Phosphate head is polar and hydrophilic as fatty acid tails are hydrophobic and non
polar
 Phospholipid arrange themselves so that heads are in water and the tails are away
from the water.
 Bilayers close in on itself so there are no edges with exposed Hydrocarbon Tails.

Fluid Mosaic model

 Cell surface membrane contains protein and cholesterol.

 Cholesterol reduces fluidity by preventing movement of phospholipids.
  Glycoprotein act as antigens and recetors
 Glycolipids help cells recognize each other.
 They are both outside of membrane
 Proteins in the membrane have hydrophobic areas and those will be within the
Bilayer.
 Presence of proteins gives the membrane of mosaic look and the movement of
proteins leads to its being the more unsaturated fatty acids called fluid.

Diffusion

 Small uncharged molecules

 Hydrophobic molecules
 Passive- no energy needed
 Substance move from a high to low concentration till equilibrium is reached.

Faciliated Diffusion

 Movement of large hydrophilic molecules or ions

 Through channel proteins or via carrier proteins that change the shape
 Passive- no energy needed
 Substance move from a high to low concentration till equilibrium is reached.

Osmosis

 Net movement of free water molecules from a high concentration of water to a low
concentration through a phospholipid bilayer.

Active transport

 Movement of molecules or ions against a concentration gradient.

 From a low to high concentration through proteins change shape.

Endocytosis

 Bulk transport of substances into the cell, using vesicles created by the cell
membrane.

Exocytosis

 Bulk transport of substances out of cell: vesicles fuse the membrane and release
their contents
 DNA and RNA
 DNA made up of lots of monomers called nucleotides.
 Joined together in condensation reaction to form a polynucleotide chain.
 DNA made up of 2 Polynucleotide twisted into a double helix.
 Nucleotide consists of phosphate, deoxyribose sugar and a base.
 2 strands are held together by hydrogen bonds between bases.

RNA different to DNA

 RNA is a single polynucleotide chain as Dna is double

 RNA contains ribose sugar as DNA contains deoxyribose.
 RNA contains uracil instead of thymine.

Genetic cod
 Genetic code is the sequence of bases in DNA that is read as a Treiplet code in
which 2 bases code for one amino acid.
 Several triplets code for the same amino acid
 A gene is a section of DNA with a specific sequence of bases that codes for a
specific sequence of amino acids forming a polypeptide bond

Protein Synthesis

The sequence of bases in the DNA of the chromosomes acts as a coded

recipe for making proteins.

TRANSCRIPTION

 occurs in the nucleus, catalysed by RNA polymerase

 DNA helix unwinds, hydrogen bonds break and RNA nucleotides pair with the
exposed bases on the template strand of the DNA

 3 bases on the DNAtriplet) are transcribed into 3 bases on the RNA (codon)

 the messenger RNA (mRNA) molecule formed enters the cytoplasm through a
nuclear pore
TRANSLATION

 occurs on the ribosomes of the rough endoplasmic reticulum

 the beginning of the sequence is always marked with the start codon AUG which
codes for the amino acid methionine

 a transfer RNA molecule (tRNA) with 3 bases exposed (an anticodon) pairs with a
specific codon on the mRNA

 attached to the tRNA molecule is a specific amino acid

 the amino acids, arranged in the order dictated by the mRNA codons, are joined with
peptide bonds to form a polypeptide

 a stop codon signals the last amino acid in the polypeptide chain

Protein Structure

 The amino acid monomers join together in a condensation reaction to form peptide
bonds.
 The polymer formed is called a polypeptide.
 Proteins are made up of one or more polypeptides.
 Primary structure the sequence of amino acids in the polypeptide chain

 Secondary structure the shape the molecule folds into as a result of hydrogen
bonding between the C=O of one amino acid and the N-H of the amine group of
another –an helix or a pleated sheet

 Tertiary structure the final 3D shape of the molecule, held together by ionic
bonds, interactions between hydrophilic R groups and strong disulphide bridges
between R groups containing sulphur
 Quaternary structure-if the protein contains more than one polypeptide chain
 Fibrous proteins remain as long chains, often with several polypeptides cross-linked
for extra strength.
 They are insoluble and are important structural molecules eg keratin, collagen.
 Globular proteins are folded into a compact spherical shape.
  They are soluble and are important metabolic molecules eg enzymes, antibodies and
some hormones.

Enzymes

 Enzymes are globular proteins which act as catalysts. They speed up chemical
reactions by lowering the activation energy, and remain unchanged at the end of the
reaction.
 Part of the molecule is a specifically shaped active site, into which a substrate fits to
form an enzyme-substrate complex.
 The induced fit hypothesis describes the active site moulding around the substrate
once it is in place.

 An increase in temperature (and therefore an increase in the kinetic energy of the

molecules) increases the likelihood of a collision between enzyme and substrate
molecules.
 The rate of reaction increases.
 Beyond the optimum temperature, the increased vibration of the atoms in the
protein molecule break the bonds maintaining the tertiary structure.
 The active site of the enzyme is irreversibly destroyed or denatured.
 pH changes around the enzymes optimum pH, alter the charge distribution in the
active site, reducing the compatibility of enzyme and substrate.
 Tertiary structure bonds are again affected and extreme changes will denature the
enzyme.
 An increase in either substrate or enzyme concentration will increase the rate of
reaction until the other acts as a limiting factor.
 Only molecules with a complementary shape will fit into active sites . The enzymes
are very specific and will only catalyse one type of reaction this is the lock and key
hypothesis.
 Activation energy is lowered by enzymes by breaking bonds in the substrate
molecule and this getting the reaction started.

Semi conservative Replication

How does DNA replication occur?

DNA copying or replication must occur before a cell divides to ensure that daughter
cells receive a copy of the genetic code.

 DNA double helix unwinds

  hydrogen bonds between the base pairs break
 free DNA nucleotides line up along side each strand
 hydrogen bonds form between complementary bases
 DNA polymerase links adjacent nucleotides
 2 identical DNA double helices are formed by this semi-conservative replication

Mutation and CF

All of the mutation affect the CFTR protein in some way. That makes it faulty. Most common
mutation on chromosome 7, it results in the loss of an amino acid and results as incorrect
folding of the CFTR protein.

Mistakes in Replication

A mistake in the trna could produce mrna with an incorrect codon: this would only result in a
faulty protein on that one occasion, in that one cell. It is mistakes in DNA replication as cells
divide that leads to inherited conditions.