Martini Chapter 2 - Part 2

Carbohydrates 1:2:1 ratio
1. contain carbon, hydrogen and oxygen in a 1:2:1 ratio
2. Monosaccharides
  1. Simple sugars
  2. contains 3 to seven carbon atoms
  3. isomers have the same molecular formula but a different arrangement in space
3. Disaccharides and Polysaccharides
  1. 2 simple sugars joined together are disaccharides
  2. condensation reactions occur to join simple sugars together to form dissaccharides and polysaccharides, it requires the removal of a water molecule
  3. di and polysaccharides have to be hydrolysed before the energy stored in the simple sugars can be used
  4. polysaccharides are more than 2 simple sugars joined together
Lipids 1:2 ratio
1. they contain carbon to hydrogen in the ratio 1:2, they also contain oxygen.
2. most lipids are insoluble
3. lipids are an important energy storage providing double that of carbohydrates
4. when there are excess lipids they are stored as fat reserves
5. Fatty Acids
  1. long carbon chains with hydrogen atoms attached
  2. one end of the chain is a carboxyl group
  3. the carboxyl group is the only part of the molecule that reacts with water as it is the only hydrophilic part of the molecule
  4. saturated fatty acids have no double carbon carbon bonds there is complete saturation of hydrogen atoms
  5. unsaturated fatty acids have double carbon carbon bonds
  6. monounsaturated means there is only one double bonds
  7. polyunsaturated means there are multiple double bonds
6. Eicosanoids
  1. lipids derived from arachidonic acid - a fatty acid that must be absorbed in the diet as it can't be made in the body
  2. Leukotrienes are produced mainly by cells that coordinate responses to injury and disease
  3. Prostaglandins are short chain fatty acids that have a ring of 5 carbons.
    1. They are released by cells to coordinate local cellular activities
    2. local hormones, they only effect the area they are released in
7. Glycerides
  1. fatty acids are joined to a backbone of glycerol
  2. the number of fatty acids determines whether it is a mono, di or tri glyceride
  3. Energy Source - they can be broken down into their parts to provide energy
  4. Insulation - fat deposits under the surface of the skin act as insulation
  5. Protection - a fat deposit around an organ provides a cushion against trauma
8. Phospholipids and Glycolipids
  1. A phospholipid is a diglyeride that is attached to a nonlipid group by a phosphate group
  2. A glycolipid is a carbohydrate attached to a diglyceride
  3. the heads of both are hydrophilic and the tails hydrophobic so a micelle forms
  4. A bylayer can be formed to make the membrane of a cell, it is mostly made of phospholipids
9. Steriods
  1. large lipid molecules that share a distinctive carbon framework
  2. the bits that make them different are the different groups that attach to them
  3. the plasma membrane contains cholesterol which is needed to maintain the plasma membrane
  4. steriod hormones are involved in sexual function
  5. steriod hormones are important in the regulation of tissue metabolism and mineral balance
  6. derivatives called bile salts are required for the processing of dietary fats
Proteins are formed from amino acids
1. Types
  1. Structural - create a 3D framework for the body
  2. Contractile - responsible for muscle contraction
  3. Transport - molecules that can't travel in the blood are transported by a transport protein
  4. Buffering - provide a buffering system to stop pH change in the blood
  5. Enzymes - accelerate metabolic reactions
  6. Hormones - influence the actions of every cell in the body or specific organs/organ systems
  7. Defense - tough waterproof proteins to protect against the outside environment and antibodies to protect against disease
2. Protein Structure
  1. long chains of amino acids
  2. There are 20 differnt amino acids that make up all the proteins in the body
  3. Amino Acids
    1. central carbon atom
    2. hydrogen atom
    3. amino group
    4. carboxyl group
    5. R group
    6. The R group is what maes each amino acid differnt and changes the function of the amino acid
    7. water soluble
    8. form peptide bonds with each other
3. Protein Shape
  1. Primary structure - sequence of amino acids in a single polypeptide
  2. Secondary structure - formation os a simple 3D shape, a helix or a pleated sheet
  3. Tertiary structure - the secondary structure bends and folds around itself and forms a complex 3D shape uses various bonds to keep its position. The strongest bond is the disulphide bond.
  4. Quaternary structure - tertiary structures bonding with each other to form a protein complex
  5. Fibrous and Globular proteins
    1. Fibrous - extended sheets are strands. Tough, durable, insoluble and structural
    2. Globular - compact, rounded and only function when in an aqueous solution
  6. Portein Shape and Function
    1. shape determines function
    2. shape depends on the order of amino acids
    3. local environmental conditions can effect the shape of proteins e.g. pH can break bonds
4. Enzyme function
  1. reactants in enzyme reactions are substrates
  2. the active site is specific to certain substrates and weak bonds form between the 2 to help the reaction happen
  3. how it happens
    1. 1 - the substrates bond to the active site
    2. 2 - the substrates are then bonded together in the enyzme substrate complex
    3. 3 - the binding of the substrates changes the shape of the active site
    4. 4 - the enzyme releases the product and starts all over again
  4. Characteristics
    1. Specificity - enzymes can only catalyze specific reactions because of their unique active sties. There are multiple enzymes that can catalyze the same reaction that are called isozymes.
    2. Saturation limits - the rate of reaction is limited by the concentration of both enzyme and substrate. The higher the concentration the higher the chance of a successsful collison and reaction taking place.
    3. Regulation - enzymes are effected by changes in the environment so the cell can change them to alter whether the enzyme is active or inactive
  5. Cofactors and Enzyme Function
    1. cofactor - ion or molecule that must bind to the enzyme before the substrate can
    2. cofactors alter the shape of the active site
    3. Coenzymes - nonproteins organic molecules that act as cofactors
  6. Temperature and pH on enzyme action
    1. optimum conditions exist for enzymes and if the conditions stay far from the set point then the enzyme will stop working and in extreme conditions will denature
    2. denature - an irriversable change in the structure of an enzyme that means it no longer functions
5. Glycoproteins and Proteoglycans
  1. combinations of proteins and carbohydrates
  2. glycoproteins - large proteins with small carbohydrate groups
  3. GPs are antiobdies, enzymes, hormones or protein components of blood plasma
  4. glycoproteins in plasma membranes identify normal and abnormal cells and start the immune response
  5. GPs also secrete mucins that absorb water to become mucus
  6. Proteoglycans are polysaccharides linked to polypeptides
DNA and RNA
1. nucleic acids - organic molecules made up of carbon, hydrogen, oxygen, nitrogen and phosphorus
2. DNA is the building blocks to life they code for everything in the body and all the characteristics that make people different
3. RNA is used to copy DNA so the information stored on the DNA can be used to make proteins
4. Structure of Nucleic acids
  1. Nucleotides - pentose sugar, phosphate group and nitrogenous base
  2. the pentose sugar is either ribose (RNA) or deoxyribose (DNA)
  3. the 5 bases
    1. T - thymine
    2. A - adenine
    3. G - guanine
    4. C - cytosine
    5. U - uracil
  4. A and G are purines - double ringed molecules
  5. T, C and U are pyrimidines - single ringed molecules
  6. T is only found in DNA and U only in RNA
  7. The phosphate group and sugar form the backbone of the DNA (the sides of the ladder)
  8. The bases form the rungs of the ladder with A and T bonding and C and G bonding only
5. RNA and DNA
  1. RNA is a single chain of nucleotides
  2. there are 3 types of RNA: mRNA - messenger, tRNA - transfer, rRNA - ribosomal
  3. DNA is a double strand of nucleotides held together with hydrogen bonds
  4. Complementary base pairs are the only pairs that occur A and T(or U), C and G.
ATP
1. ATP can be broken down to ADP and then AMP releasing energy each time
2. high energy compound
3. the attachment of a phosphate group on to another molecule is called phosphorylation
4. ATP is made up of adenine bonded to ribose which is then bonded to a chain of 3 phosphates
5. to convert from ADP to ATP you have to use ATPase

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Martini Chapter 2 - Part 2

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