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BIOCHEMISTRY

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Title: BIOCHEMISTRY


1
BIOCHEMISTRY
2
Macromolecules
  • Building Blocksof Life

3
first a little review
4
Macromolecules
  • Smaller organic molecules join together to form
    larger molecules
  • macromolecules
  • 4 major classes of macromolecules
  • carbohydrates
  • lipids
  • proteins
  • nucleic acids

5
Polymers
  • Long molecules built by linking repeating
    building blocks in a chain
  • monomers
  • building blocks
  • repeated small units
  • covalent bonds

Dehydration synthesis
6
How to build a polymer
  • Synthesis
  • joins monomers by taking H2O out
  • 1 monomer provides OH
  • other monomer provides H
  • together these form H2O
  • requires energy enzymes

Dehydration synthesis
Condensation reaction
7
How to break down a polymer
  • Digestion
  • use H2O to breakdown polymers
  • reverse of dehydration synthesis
  • cleave off one monomer at a time
  • H2O is split into H and OH
  • H OH attach to ends
  • requires enzymes

Hydrolysis
Digestion
8
Bonding
  • Covalent Bonds
  • atoms share electrons.
  • 2 kinds

9
  • Nonpolar covalent bonds
  • electrons shared evenly between similar atoms
  • bond is strong
  • Ex O2, N2

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  • Polar covalent bond
  • Electrons shared unevenly between dissimilar
    atoms
  • one atom pulls electrons more
  • Gives a slightly negative charge
  • Ex H20

12
  • Hydrophilic (polar) molecules
  • have polar covalent bonds
  • dissolve in water
  • dissociate easily
  • Ex glucose, amino acids

13
  • Hydrophobic (nonpolar) molecules
  • mainly nonpolar covalent bonds
  • do not dissolve in water (have few charges).
  • Ex Lipids (fats)

14
  • Ionic Bonds
  • Electrons not shared
  • one or more electrons are transferred from one
    atom to another.

15
  • Transferring atom ()
    cation
  • Receiving atom (-) anion
  • NaCl is an example

16
  • Ionic bonds
  • weaker than covalent
  • dissociate when dissolved in H2O.
  • Form hydration spheres

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Note orientation of water molecules
H2O
19
  • Hydrogen bonds
  • weak bonds
  • account for
  • shape (due to folding) of large proteins
  • holds DNA ladders together
  • physical properties of water (like surface
    tension and capillary action).

20
  • Disulfide bonds
  • found in proteins
  • cause shape of proteins (folding and twisting of
    protein shapes).

21
Chemical Reactions
  • Synthesis
  • results in the formation of new bonds
  • requires energy
  • wound healing, tissue growth
  • Decomposition
  • results in bond breakage
  • energy is released as heat or captured for
    storage digestion

22
Types of Rxns
Synthesis Reaction more complex chemical
structure is formed requires energy (wound
healing, tissue growth) A B AB
Decomposition Reaction chemical bonds are
broken to form a simpler chemical structure rls
energy (digestion) AB A B
Exchange Reaction chemical bonds are broken and
new bonds are formed AB CD AD CB
Reversible Reaction the products can change
back to the reactants A B n AB
23
Organic vs. Inorganic
24
  • Organic compounds
  • contain covalently bonded carbon atoms
  • include macromolecules
  • carbohydrates
  • Lipids
  • Proteins
  • nucleic acids

25
  • Most macromolecules include a carbon core with
    functional groups attached.
  • arrangements of atoms giving carbon core unique
    chemical properties

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  • Inorganic compounds
  • required, but not made by, living things
  • contain no carbon
  • include acids, bases, water, salts, minerals

30
Inorganic Compounds
  • Water
  • accounts for 60 80 of cell contents
  • very versatile and vital

31
  • Universal solvent (because it is a polar
    molecule)
  • No chemical reactions unless in solution
  • Dissolved compounds can be brought to cells (via
    blood) or move about cell cytoplasm

32
  • Exhibits cohesion water molecules stick together
    due to the hydrogen bonds.

33
  • Exhibits adhesion
  • water molecules stick to other molecules thereby
    keeping things dissolved
  • Polarity of water causes hydration layers with
    other molecules as (-) ends of water surround and
    enclose the () ends of other molecules and vice
    versa.

34
  • Has a high heat capacity
  • large amounts of heat are needed to raise the
    temperature of water, so water bodies have stable
    temperatures
  • Body temps can be maintained
  • transfer of heat from warm to cool body parts.

35
  • Has a high boiling point
  • Much energy is needed to pull water molecules
    apart
  • since water rarely boils in nature, living
    systems are spared.

36
  • Major transport medium of body blood
  • Major component of body lubricants synovial
    fluid, mucus, etc.
  • Cushioning cerebrospinal fluid, amniotic fluid

37
  • Salts ionic compounds consisting of () and (-)
    ions other than H and OH-
  • become electrolytes in body when dissolved
  • conduct electricity in bodily functions such as
    muscle contraction and nerve conduction.

38
  • Important to bone and teeth hardness.
  • Forms parts of hemoglobin molecule of RBCs.

39
  • Acids
  • Taste sour
  • React with metals
  • Concentration of H ions that determine acidity
  • Proton () donors produced by the body (gastic
    acid) or produced as a by-product (hydrogen
    peroxide)

40
  • Bases
  • Taste bitter
  • Feel slippery
  • Proton acceptor, produced by the body
    (bicarbonate) or as a by-product of metabolism
    (ammonia)

41
  • Buffers
  • Substances that maintain the pH constancy of body
    fluids
  • Act as a H reservoir add or remove excess H

42
Organic Compounds
  • Contain carbon which is a unique molecule.
  • Carbon bonds with itself and/or other molecules,
    covalently.
  • Often found in chains (straight or branched),
    rings, folded sheets, etc..

43
  • makes carbon versatile
  • The way carbons are bonded together determines
    type of organic compound
  • carbohydrate, lipid, protein, nucleic acid, etc.

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Carbohydrates
  • Known as sugars, CH2O
  • classified by size
  • named according to the number of carbons in the
    molecule (triose, tetrose, pentose, hexose, etc.)
    monomer monosaccharide (Latin sacchron means
    sugar)
  • major energy source for the human body

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  • Disaccharides (C12H22O11) known as double
    sugars
  • formed when 2 monosaccharides are joined together
    by dehydration synthesis
  • done so sugars can be transported.

49
  • for example
  • sucrose (table sugar)
  • lactose (milk sugar)
  • maltose (grain sugar)
  • created through dehydration synthesis of pairs of
    monosaccharides.

50
  • Polysaccharides
  • known as complex sugars
  • formed when many monosaccharides are joined
  • act as
  • fuel for cells
  • structural components of DNA
  • cell membranes
  • cell surface receptors).

51
  • examples
  • glycogen (animal starch stored in the liver and
    muscles)
  • cellulose (structural polysaccharide of plant
    cell walls)
  • starch (plant polysaccharide

52
  • When body needs energy, it looks to the liver to
    hydrolize glycogen (stored starch) and release
    the resulting monosaccharide to the cells.

53
  • the cells, in turn, release energy from bonds of
    monosaccharide
  • energy that is released is converted to another
    energy compound called ATP.

54
Lipids
  • Commonly called fats
  • insoluble in polar solvents (like water)
  • soluble in nonpolar organic solvents like
    alcohol, ether, gasoline
  • commonly attached to proteins in the bloodstream
    so they can travel in the aqueous plasma even
    though they are hydrophobic

55
  • composed of CHO but with a lower oxygen ratio
    than carbohydrates
  • classified by their solubility.
  • Ex include fats, oils, and waxes

56
  • Triglycerides (fats)
  • composed of 3 fatty acids (carbon-hydrogen chain)
    and 1 glycerol (sugar) through
  • dehydration synthesis into an E shape.
  • large molecule which must be broken down in order
    to release the large amount of stored energy.

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  • usually stored under the skin as fat
  • can also collect in the lining of blood vessels
    and cause blockages
  • act as good cushions, insulators and a
    concentrated source of energy

59
  • Fatty acids are classified as
  • saturated (originating from animals and having
    all available hydrogens atoms which make them
    harder to metabolize)
  • unsaturated lacking some hydrogen atoms
    contains double bonds

60
                                                                                                                                                                                                                                                                          

61
  • polyunsaturated (originating from plants)
  • Hydrogenating oils makes them saturated and solid

62
  • Phospholipids
  • complex lipids
  • modified triglycerides composed of 2 fatty acids
    and a phosphorus chain
  • used to build cell membranes.

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  • Steroids
  • lipid composed of ringed hydrocarbons
  • Examples
  • cholesterol which is the precursor for many
    hormones (like estrogen, progesterone, and
    testosterone)
  • vitamin D
  • bile salts.

66
  • Prostaglandins
  • tissue hormone
  • lipid responsible for
  • blood vessel diameter
  • Ovulation
  • uterine contraction
  • inflammation reactions
  • blood clotting

67
  • Proteins
  • 10 30 of cell mass composed of CHONPS
  • monomers amino acids (20 commonly known)
  • linked together by peptide bonds to form
    polypeptides.
  • Strings of polypeptides protein.
  • Average proteins are 50,000 aa long

68
  • protein versatility results from the various
    combinations and numbers of amino acids as well
    as the structural shape they take on (primary,
    secondary, tertiary, quaternary) shape confers
    properties.

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  • Structural proteins
  • primary and secondary structures
  • linear or helical
  • Insoluble
  • Stable
  • form body parts like collagen, keratin, elastin,
    bones, tendons, ligaments, cartilage, hair,
    nails, etc.

71
  • Functional proteins
  • tertiary, quaternary structures
  • water soluble
  • Mobile
  • chemically active
  • include antibodies, hormones, enzymes

72
  • Denaturing of proteins functional proteins are
    highly susceptible to heat and pH (due to the
    weakness of the hydrogen bonds holding together
    their structure)

73
  • heat denaturation is irreversible once the
    arrangement of the molecule (and its composing
    atoms) is disrupted, it is no longer active.

74
  • Enzymes
  • proteins
  • act as biological catalyst
  • Lower activation energy of the substrate
  • Not destroyed or used up

75
  • some are proteins needing activation (cofactor)
    from a vitamin or mineral
  • named according to substrate it catalyzes ex
    maltase hydrolyzes maltose most enzymes have an
    ase ending.

76
  • Operate in a very narrow pH, temperature and
    ionic range.
  • can vary from enzyme to enzyme ex enzymes in
    the stomach vs. enzymes in the blood

77
  • Enzymes are substrate specific one enzyme for
    each type of substrate
  • Enzymes are reusable

78
  • Enzymes have an activation site to which the
    substrate bonds. Any change in this site will
    render the enzyme inactive denaturation

79
  • Naming Enzymes
  • Name of substrate affected with ase on the end
    ex sucrase, lactase, protease
  • According to kind of chemical reactions catalyzed

80
Factors Influencing Enzyme Activity
  • Temperature
  • pH
  • Ionic concentration
  • Substrate concentration?
  • Enzyme concentration?
  • Competitive inhibitors
  • Noncompetitive inhibitors
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