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Martini Chapter 2 - Part 2

06watkinse BMSC1110 Undergraduate Degree English

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Martini Chapter 2 - Part 2

  1. Carbohydrates 1:2:1 ratio

    • contain carbon, hydrogen and oxygen in a 1:2:1 ratio
    • Monosaccharides
      • Simple sugars
      • contains 3 to seven carbon atoms
      • isomers have the same molecular formula but a different arrangement in space
    • Disaccharides and Polysaccharides
      • 2 simple sugars joined together are disaccharides
      • condensation reactions occur to join simple sugars together to form dissaccharides and polysaccharides, it requires the removal of a water molecule
      • di and polysaccharides have to be hydrolysed before the energy stored in the simple sugars can be used
      • polysaccharides are more than 2 simple sugars joined together
  2. Lipids 1:2 ratio

    • they contain carbon to hydrogen in the ratio 1:2, they also contain oxygen.
    • most lipids are insoluble
    • lipids are an important energy storage providing double that of carbohydrates
    • when there are excess lipids they are stored as fat reserves
    • Fatty Acids
      • long carbon chains with hydrogen atoms attached
      • one end of the chain is a carboxyl group
      • the carboxyl group is the only part of the molecule that reacts with water as it is the only hydrophilic part of the molecule
      • saturated fatty acids have no double carbon carbon bonds there is complete saturation of hydrogen atoms
      • unsaturated fatty acids have double carbon carbon bonds
      • monounsaturated means there is only one double bonds
      • polyunsaturated means there are multiple double bonds
    • Eicosanoids
      • lipids derived from arachidonic acid - a fatty acid that must be absorbed in the diet as it can't be made in the body
      • Leukotrienes are produced mainly by cells that coordinate responses to injury and disease
      • Prostaglandins are short chain fatty acids that have a ring of 5 carbons.
        • They are released by cells to coordinate local cellular activities
        • local hormones, they only effect the area they are released in
    • Glycerides
      • fatty acids are joined to a backbone of glycerol
      • the number of fatty acids determines whether it is a mono, di or tri glyceride
      • Energy Source - they can be broken down into their parts to provide energy
      • Insulation - fat deposits under the surface of the skin act as insulation
      • Protection - a fat deposit around an organ provides a cushion against trauma
    • Phospholipids and Glycolipids
      • A phospholipid is a diglyeride that is attached to a nonlipid group by a phosphate group
      • A glycolipid is a carbohydrate attached to a diglyceride
      • the heads of both are hydrophilic and the tails hydrophobic so a micelle forms
      • A bylayer can be formed to make the membrane of a cell, it is mostly made of phospholipids
    • Steriods
      • large lipid molecules that share a distinctive carbon framework
      • the bits that make them different are the different groups that attach to them
      • the plasma membrane contains cholesterol which is needed to maintain the plasma membrane
      • steriod hormones are involved in sexual function
      • steriod hormones are important in the regulation of tissue metabolism and mineral balance
      • derivatives called bile salts are required for the processing of dietary fats
  3. Proteins are formed from amino acids

    • Types
      • Structural - create a 3D framework for the body
      • Contractile - responsible for muscle contraction
      • Transport - molecules that can't travel in the blood are transported by a transport protein
      • Buffering - provide a buffering system to stop pH change in the blood
      • Enzymes - accelerate metabolic reactions
      • Hormones - influence the actions of every cell in the body or specific organs/organ systems
      • Defense - tough waterproof proteins to protect against the outside environment and antibodies to protect against disease
    • Protein Structure
      • long chains of amino acids
      • There are 20 differnt amino acids that make up all the proteins in the body
      • Amino Acids
        • central carbon atom
        • hydrogen atom
        • amino group
        • carboxyl group
        • R group
        • The R group is what maes each amino acid differnt and changes the function of the amino acid
        • water soluble
        • form peptide bonds with each other
    • Protein Shape
      • Primary structure - sequence of amino acids in a single polypeptide
      • Secondary structure - formation os a simple 3D shape, a helix or a pleated sheet
      • 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.
      • Quaternary structure - tertiary structures bonding with each other to form a protein complex
      • Fibrous and Globular proteins
        • Fibrous - extended sheets are strands. Tough, durable, insoluble and structural
        • Globular - compact, rounded and only function when in an aqueous solution
      • Portein Shape and Function
        • shape determines function
        • shape depends on the order of amino acids
        • local environmental conditions can effect the shape of proteins e.g. pH can break bonds
    • Enzyme function
      • reactants in enzyme reactions are substrates
      • the active site is specific to certain substrates and weak bonds form between the 2 to help the reaction happen
      • how it happens
        • 1 - the substrates bond to the active site
        • 2 - the substrates are then bonded together in the enyzme substrate complex
        • 3 - the binding of the substrates changes the shape of the active site
        • 4 - the enzyme releases the product and starts all over again
      • Characteristics
        • 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.
        • 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.
        • Regulation - enzymes are effected by changes in the environment so the cell can change them to alter whether the enzyme is active or inactive
      • Cofactors and Enzyme Function
        • cofactor - ion or molecule that must bind to the enzyme before the substrate can
        • cofactors alter the shape of the active site
        • Coenzymes - nonproteins organic molecules that act as cofactors
      • Temperature and pH on enzyme action
        • 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
        • denature - an irriversable change in the structure of an enzyme that means it no longer functions
    • Glycoproteins and Proteoglycans
      • combinations of proteins and carbohydrates
      • glycoproteins - large proteins with small carbohydrate groups
      • GPs are antiobdies, enzymes, hormones or protein components of blood plasma
      • glycoproteins in plasma membranes identify normal and abnormal cells and start the immune response
      • GPs also secrete mucins that absorb water to become mucus
      • Proteoglycans are polysaccharides linked to polypeptides
  4. DNA and RNA

    • nucleic acids - organic molecules made up of carbon, hydrogen, oxygen, nitrogen and phosphorus
    • DNA is the building blocks to life they code for everything in the body and all the characteristics that make people different
    • RNA is used to copy DNA so the information stored on the DNA can be used to make proteins
    • Structure of Nucleic acids
      • Nucleotides - pentose sugar, phosphate group and nitrogenous base
      • the pentose sugar is either ribose (RNA) or deoxyribose (DNA)
      • the 5 bases
        • T - thymine
        • A - adenine
        • G - guanine
        • C - cytosine
        • U - uracil
      • A and G are purines - double ringed molecules
      • T, C and U are pyrimidines - single ringed molecules
      • T is only found in DNA and U only in RNA
      • The phosphate group and sugar form the backbone of the DNA (the sides of the ladder)
      • The bases form the rungs of the ladder with A and T bonding and C and G bonding only
    • RNA and DNA
      • RNA is a single chain of nucleotides
      • there are 3 types of RNA: mRNA - messenger, tRNA - transfer, rRNA - ribosomal
      • DNA is a double strand of nucleotides held together with hydrogen bonds
      • Complementary base pairs are the only pairs that occur A and T(or U), C and G.
  5. ATP

    • ATP can be broken down to ADP and then AMP releasing energy each time
    • high energy compound
    • the attachment of a phosphate group on to another molecule is called phosphorylation
    • ATP is made up of adenine bonded to ribose which is then bonded to a chain of 3 phosphates
    • to convert from ADP to ATP you have to use ATPase

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Undergraduate Degree BMSC1110 (Martini reading) Mind Map on Martini Chapter 2 - Part 2, created by 06watkinse on 10/10/2013.
Created by
06watkinse · Oct 2013
Updated
Feb 19, 2016
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  • Created by 06watkinse · Oct 10, 2013
  • Copied by 06watkinse · Oct 10, 2013
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