Biology Ch5

  1. Macromolecule
    Large Molecules
  2. Whar are the 4 large molecule groups?
    Whick one is not a macromolecule?
    • Carbohydrates
    • Proteins
    • Nucleic Acids
    • Lipids - not a macromolecule group
  3. Polymers
    • Greek - Polys (many) and meris (part) Many parts
    • Long molecule consisting of many similar or identical builing blocks linked by covalent bonds (train consists of cars)
  4. Monomers
    Smaller molecules that often make up the building blocks of polymers
  5. dehydration synthesis
    • Building
    • also called a condensation reaction or a dehydration reaction
    • Two monomers covalently bonded to one another thorugh the loss of a water molcule
    • Both momomers contribute part of the water molecule that is lost (one contributes -OH and one -H)
    • Energy is used
    • 1 molecule of water is realeased
    • Extra Energy is stored in the bonds
    • Some energy is lost as heat
  6. Hydrolysis
    • Breaking Down
    • Greek hydro (water) lysis (break) To break down using water
    • Bonds are broken by the attition of a water molecule and a polymer separates into monomers
    • 1 water molecule is used
    • 1 bond is broken
    • entergy is relased
  7. Carbohydrates
    Charbohydrates -Sugars and polymers of sugars
  8. Monosaccharides
    • simple sugars
    • Glucose is the most common -C6H12O2
    • Fructose is a isomer of glucose
    • A sugar molecule has a corbonyl group and multible hydroxyl groups. Depending on location of carbonyl group the sugar is either aldose (aldehyde sugar) or ketose (ketone sugar)
  9. How are sugars classifies?
    • Size of the carbon skeleton - ranges from three to seven carbons long
    • Glucose, fructose have six carbons are called hexoses
    • three carbon sugars are called trioses
    • five carbon sugars are called pentoses
  10. Disaccharides
    • double sugars, two monosaccharides joined by glycosidic linkage ( a covalent bond by dehydration synthesis)
    • Maltose, Sucrose (table sugar), lactose
  11. Polysaccharides
    Two types of polysaccharides
    Macromolecules, polymenrs composed of many sugars joined by glycosidic linkage

    • Storage Polysaccharides
    • Structure Polysaccharides
  12. Storage Polysaccharides
    • Plants store surplus glucose as a polysaccharide called Starch
    • Animals store a polysacchride called Glycogen - stored as granules in the liver and muscles
  13. Structural Polysaccharides
    • Organisms build strong materials from structural polysaccharides
    • Plants - Cellulose (polysaccharide) is the major component of the tough walls that enclose plant cells- insoluable fiber **Cellulose is the most abundant organic compound on earth
    • Animals - Chitin - exoskeleton of insects and crustaceans
  14. Lipids
    • Not Macromolecules
    • Mostly Hydrophobic - no monomers
    • Fats, Steroids, Phospholipids, waxes
  15. Fats
    • Lipid - hydrophobic - not a macromolecule
    • Fats are storage for animals - can store twice as much potential energy than other storage
    • A fat is formed by a glycerol (alcohol w/ 3 carbons-each with a hydroxly group) with three fatty acids (Long carbon chains -16 to 18 carbons- with a carboxyl group (acid) - triglyceride
    • (Carbon chain surrounded by Hydrogen)
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  16. Saturated Fat
    • Normally solid at room temperature
    • Animal Fat - bacon fat, butter, lard
    • Hydrocarbons - where there are no double bonds between carbons then as many hydrogen atoms as possible are bonded to the carbon skeleton - saturated with hydrogen
    • The "tails" of fat have no double bonds are very flaxible - can be tightly packed (solid)
  17. Unsaturated Fat
    • Oils - liquid at room temperature
    • Hydrocarbon - has one or more double carbon bonds - kinks where Cis double bonds forms -
    • tails are not able to be tightly packed together so stays as liquid
  18. Trans fats
    • Unsaturated fats are atrifically pumped full of hydrogen atoms to make them saturated. This process makes saturated fats and unsaturated fats with a trans double bond.
    • Saturated and Trans fats cause plaque (deposits within the wall off a blood vessel that cause invard bulges and decreases blood flow)
  19. Phospolipids
    • Make up the cell membrane - essential for cells
    • One glycerol (alcohol w/3 carbons each has a hydroxyl group) attached to two fatty acids (hydrocarbon with a carboxyl group) third hydroxyl group is attached to a phosphate group
    • Polar heads are hydrophyllic
    • Hydrocarbon tails are hydrophobic
    • Form a bilayer with head out and tails that is essential for call membrane
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  20. Steroids
    • Lipid - not a macromolecule - sex hormones
    • Carbon skeleton consisting of 4 fused rings
    • Cholesterol is an essential steroid in the liver that synthesizes other steroids (sex hormones)
    • Secondary sexual Characteristics - artifical steroids cause wrong sex hormones to be produced - women grow hair on face, mens testicles shrink
  21. Protein
    • Macromolecule - can not be constructed without amino acids
    • 75,000 proteins in our body are made from different combonations of 20 Amino Acids. Every living thing has 20 amino acids.
    • Amino Acids are joined by Peptide Bonds to form Polypeptides- Peptide bonds only work for Amino Acids - the carboxyl groups of one Amino Acid joins the amino group of amother through dehydration systhesis
    • Proteins consist of one or more polypeptides twisted, folded, and coiled into a molecule of unique shape.
  22. Peptide Bonds
    • Amino Acids are joined by Peptide Bonds to form Polypeptides- Peptide
    • bonds only work for Amino Acids - the carboxyl groups of one Amino Acid
    • joins the amino group of amother through dehydration systhesis
  23. Polypeotides
    Polymers of amino acids. A protein is made of one or more polypeptide chains twisted, folded, and coiled into molecule of unique shape
  24. Two shapes of proteins
    • globular (roughly spherical)
    • fibrous (long fibers)
  25. Form and Function of Proteins
    Form equals function. Proteins are polypeptides that are folded, twisted and coiled into specific shapes for specific purposes
  26. Four levels of protein structure
    • 1)Primary structure - Unique amino acid sequence (amino end and carboxyl end) - problems if not in the right order (cicle cell anemia)
    • 2)Secondary structure - pleating, coiling and folding aided by Chaperonin - surrounds and protects the proteins that are folding. Misfolding results in Alzheimers, Parkinsons
    • 3)Tertiary structure - 3D shape - hydrophobic interations - as a polypeptide folds amino acids with hydrophobic side chains end up clusted in the middle. Mad cow disease is caused by misshapen tertiary structure
    • 4)Quarternary - 2 or more polypeptides (subunit) combine to form a unit
  27. Denaturation reaction
    • When a protein is unraveled or loses its native shape - some are irreversible. The denatured protein is biologically inactive.
    • 1)Extreme changes in temperature - ex. Ovalbumin (egg whites) when cooked
    • 2)Extreme changes in pH - body pH over 7.8 results in death
    • 3)Extreme changes in salt concentration - dehydration = high salt concentration
  28. 8 Functions of Proteins
    • 1) Enzymes - most important - speed up chemical reacions -digestive enzymes
    • 2) Structural proteins - support - hair & tentons
    • 3) Contractile proteins - movement - muscles
    • 4) Defense proteins - protect against disease - antibodies combat bacteria and viruses
    • 5) Signal proteins - Hormones - insulin (a hormone secreted by the pancreas regulates sugar in the body)
    • 6) Receptor proteins - in the cell membrane - can detect chemical signals sent by other cells
    • 7) Transport proteins - hemoglobin transports oxygen to all parts of body
    • 8) Storage proteins - storage of amino acids - ovalbumin (egg white) is amino acid source for the embryo
  29. R group
    variable group or side chain attached to an amino acid that differs with each amino acid
  30. Nucleic Acid
    • Macromolecule - enables living organisms to reproduce their complex components from one generation to the next (DNA & RNA)
    • Its monomer is a nucleotide - polymers are polynucleotides
  31. Dr. Linus Pauling
    • Nobel prize for chemistry 1954
    • Nobel prize for peace 1963
    • Only person ever to be awarded two unshared nobel prizes
    • Described alpha helix and pleated sheet in seconday protein structure

    Watson & Crick given nobel prize for structure of DNA
  32. gene
    unit of inheritance that programs the amino acid sequence of a polypeptide
  33. DNA
    • Deoxyribonucleic acid
    • genetic material that organisms inherit from their parents
    • *DNA provides directions for its own replication
    • *DNA directs RNA sysntesis and, through RNA, contols protein synthesis
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  34. Nucleotide and its 3 parts
    • Nucleotide is the building blocks of polynucleotides - Nucleic Acids
    • 1)Nitrogenous Base - pyrimadines or purine
    • 2)Pentose (5 carbon) sugar - ribose for RNA and deoxyribose for DNA
    • 3)Phosphate group
    • The porton of this group without the phosphate group is called a nucleoside (nitrogenous base and sugar)
  35. Two families of Nitrogenous bases
    • used to build nucleotides (used to build nucleic acid)
    • 1) pyrimidine - six-membered ring of carbon and nitrogen atoms
    • a) cytosine (C)
    • b) thymine (T)
    • c) Uracil (U)
    • 2) pruines - larger, six membered ring fused to a five membered ring
    • a) Adenine (A)
    • b) Guanine (G)
  36. prime (')
    sugars in a nitrogenous base are numbered - second carbon in a sugar rings is 2' (2prime) and the carbon that sticks up from the ring is a 5' carbon
  37. How are nucleotides linked to form a polynucelotide?
    • a phosphate group that links the sugars of two nucleotides (backbone with a repeating pattern of sugar-phosphate units)
    • the two end are distinctly different - one end has a phosphate attached to a 5' carbon and the other end has a hydroxly group on a 3' carbon
    • In DNA sugar-phosphate backbone on the outside with nitrogenous bases paired on the inside (links between the double helix)
    • 5' - Phosphate group
    • 3' - Hydroxly group
  38. Complementary Pairs
    • DNA
    • A - T Adenine - Thymine
    • T - A Thymine - Adenine
    • C - G Cytosine - Guanine
    • G - C Guanine - Cytosine

    • RNA
    • A - U Adenine - Urasil
    • U - A Urasil - Adenine
    • C - G Cytosine - Guanine
    • G - C Guanine - Cytosine
  39. Transcription

    • Process by which DNA synthesizes RNA
    • DNA is the boss

    • Replication - Mitosis - process by which a cell separates DNA into two identical sets
    • Replication is caused by
    • Disease
    • Damage
    • Death
    • Growth
  40. mRNA
    • messanger RNA (synthesized in the nucleus)
    • transfer RNA (fouund in the cytoplasm)
    • ribosomal RNA (found in the nucleolus)
Card Set
Biology Ch5
Lecture and Book over Chapter 5 - Macromolecules