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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
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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 alv eoli 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
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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
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Cell surface membrane contains protein and cholesterol. Cholesterol reduces fluidity by preventing movement of phospholipids.

using vesicles created by the cell membrane.no energy needed Substance move from a high to low concentration till equilibrium is reached. Endocytosis y Bulk transport of substances into the cell.no energy needed Substance move from a high to low concentration till equilibrium is reached. 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. Active transport y y Movement of molecules or ions against a concentration gradient. From a low to high concentration through protei ns change shape.y y y y y Glycoprotein act as antigens and recetors Glycolipids help cells recognize each other. Faciliated Diffusion y y y y Movement of large hydrophilic molecules or ions Through channel proteins or via carrier proteins that change the shape Passive. Exocytosis y Bulk transport of substances out of cell: vesicles fuse the membrane and release their contents . Diffusion y y y y Small uncharged molecules Hydrophobic molecules Passive. Osmosis y Net movement of free water molecules from a high concentration of water to a low concentration through a phospholipid bilayer. They are both outside of membrane Proteins in the membrane have hydrophobic areas and those will be within the Bilayer.

Nucleotide consists of phosphate. DNA made up of 2 Polynucleotide twisted into a double helix. hydrogen bonds break and RNA nucleotides pair with the exposed bases on the template strand of the DNA y 3 bases on the DNAtriplet) are transcribed into 3 bases on the RNA ( codon) y the messenger RNA (mRNA) molecule formed enters the cytoplasm through a nuclear pore . 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. catalysed by RNA polymerase y DNA helix unwinds. RNA different to DNA y y y y y y y RNA is a single polynucleotide chain as Dna is double RNA contains ribose sugar as DNA contains deoxyribose.DNA and RNA y y y y y DNA made up of lots of monomers called nucleotides. deoxyribose sugar and a base. 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. TRANSCRIPTION y occurs in the nucleus. RNA contains uracil instead of thymine. Joined together in condensation reaction to form a polynucleotide chain. 2 strands are held t ogether by hydrogen bonds between bases.

. held together by ionic bonds. Primary structure the sequence of amino acids in the polypeptide chain y 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 y y y y y Tertiary structure the final 3D shape of the molecule. are joined with peptide bonds to form a polypeptide a stop codon signals the last amino acid in the polypeptide chain y Protein Structure y y y y The amino acid monomers join together in a condensation reaction to form peptide bonds. They are insoluble and are important structural molecules eg keratin. The polymer formed is called a polypeptide. Globular proteins are folded into a compact spherical shape. Proteins are made up of one or more polypeptides. often with several polypeptides cross -linked for extra strength. 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. arranged in the order dictated by the mRNA codons.TRANSLATION y occurs on the ribosomes of the rough endoplasmic reticulum y the beginning of the sequence is always marked with the start codon AUG which codes for the amino acid methionine y a transfer RNA molecule (tRNA) with 3 bases exposed (an anticodon) pairs with a specific codon on the mRNA y attached to the tRNA molecule is a specific amino acid y the amino acids. colla gen.

Activation energy is lowered by enzymes by breaking bonds in the substrate molecule and this getting the reaction started. alter the charge distribution in the active site. They speed up chemical reactions by lowering the activation energy. Beyond the optimum temperature. pH changes around the enzymes optimum pH. An increase in temperature (and therefore an increase in the kinetic energy of the molecules) increases the likelihood of a collision between enzyme and sub strate molecules. The enzymes are very specific and will only catalys e one type of reaction this is the lock and key hypothesis. Enzymes y y y Enzymes are globular proteins which act as catalysts. antibodies and some hormones. y y y y y y y y y 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. An increase in either substrate or enzyme concentration will increase the rate of reaction until the other acts as a limiting factor. and remain unchanged at the end of the reaction. into which a substrate fits to form an enzyme-substrate complex. Tertiary structure bonds are again affected and extreme changes will denature the enzyme. The induced fit hypothesis describes the active site moulding around the substrate once it is in place. reducing the compatibility of enzyme and substrate. The active site of the enzyme is irreversibly destroyed or denatured. Only molecules with a complementary shape will fit into active sites . the increased vibration of the atoms in the protein molecule break the bonds maintaining the tertiary structure. y DNA double helix unwinds .y They are soluble and are important metabolic molecules eg enzymes. The rate of reaction increases. Part of the molecule is a specifically shaped active site.

. 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.y y y y y hydrogen bonds between the base pairs break free DNA nucleotides line up along si de 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. It is mistakes in DNA replication as cells divide that leads to inherited conditions. in that one cell. Mistakes in Replication A mistake in the trna could produce mrn a with an incorrect codon: this would only result in a faulty protein on that one occasion.