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Biochemistry. Organic Molecules. Molecules that have a carbon skeleton and covalent carbon-hydrogen bonds Can be man made. Carbon. Can form 4 covalent bonds. Allows for molecular diversity in shape and length. Miller/Urey Experiment. Review of Functional Groups.

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organic molecules
Organic Molecules
  • Molecules that have a carbon skeleton and covalent carbon-hydrogen bonds
  • Can be man made
carbon
Carbon
  • Can form 4 covalent bonds
  • Allows for molecular diversity in shape and length
review of functional groups
Review of Functional Groups
  • ID the various functional groups in the following molecules…
phosphate
Phosphate

Adenosine

slide10

Carboxyl group (COOH)

It’s a fatty acid… why acid?

slide12

Ethanol… alcohol in adult beverages

OH… looks like ____... Alcohol can make you do these types of things…

alanine
Alanine

Amino  NH2

Carboxyl  COOH (think about what this is going to do when in a solution)

What is alanine an example of? There are 20 of them.

aldehyde
Aldehyde
  • Think… formaldehyde stinks… put it on the end!
  • Ketone trick?
proteins
Proteins
  • More than 50% of the dry weight of an organism
  • Made of smaller subunits (monomers) amino acids
amino acids
Amino Acids
  • Amino Group
  • Carboxyl Group
  • Hydrogen Atom
  • R group (20 different  different properties)
proteins1
Proteins
  • Amino Acids connected by Peptide Bonds
  • Dipeptide
  • Polypeptide
slide21

Groove

(a) A ribbon model

Figure 5.19

Protein Structure

protein structure
Protein Structure
  • Primary- Chain of amino acids
  • Secondary- Due to H-Bonds between amino acids
protein structure1
Protein Structure
  • Tertiary- “Active” Shape
    • H-Bonds between R-groups
    • Ionic Bonds between R- groups
    • Nonpolarity (pushed together by water)
    • Sulfur bridges (covalent bond between 2 cysteines)
    • Van der waals attractions
protein structure2
Protein Structure
  • Quarternary Structure
    • Joining of two or more polypeptide chains
slide27

Groove

Figure 5.19

(a) A ribbon model

slide28

Directions

  • Pick up an amino acid sequence, scissors, and tape
  • Grad JUST the amino acids you will need from the back and 9 water molecules (they’re in sheets of 13 so cut them apart)
  • Assemble your amino acids showing what must be removed to put your amino acids together
  • ANSWER THE FOLLOWING 1/GROUP (put both names on)
slide29

Questions to turn in at the end of the period

  • What is the polymer that is created when amino acids are bonded together?
  • What 2 functional groups are present on EVERY amino acid (name & draw)
  • If all amino acids share 2 functional groups then why are they different? EXPLAIN.
  • What reaction must occur in order to break a chain of amino acids into individual amino acids?
  • What must happen to a chain of amino acids to make it a protein?
groups
Groups
  • Catalysts- Enzymes  speed up rates of chem. rxns
  • Structural- for support; hair, silk, connective tissue
  • Storage- source of amino acids for young
groups1
Groups
  • Transport- of other substances
  • Hormonal- coordinates and directs regulation of organisms
  • Receptors- decide what comes in/out of cells
groups2
Groups
  • Transcription factors- tells cells what to make
  • Motor- make up muscles, cilia, flagella, etc
  • Defensive- antibodies
enzymes
Enzymes
  • Organic Catalysts
  • Lower Activation Energy
  • May need a coenzyme in order to function
isomers
Isomers
  • Isomers- Molecules with same atoms but different arrangement and properties
functional groups
Functional Groups
  • Groups of atoms that give a molecule specific properties
hydroxyl
Hydroxyl
  • Alcohols
carbonyl
Carbonyl
  • Ketones, formaldehyde
carboxyl
Carboxyl
  • “Organic” Acids
amino
Amino
  • Amino Acids
sulfhydryl
Sulfhydryl
  • Found in proteins
phosphate1
Phosphate

OR

  • Phospholipids, Nucleotides
building macromolecules
Building Macromolecules
  • Monomers- Small organic molecules that can be linked together
  • Polymers- Big things (monomers linked together)
building
Building
  • Condensation (dehydration synthesis): connects 2 molecules.
  • One molecule loses an H, the other loses an OH
  • One water molecule is formed
taking apart
Taking Apart
  • Hydrolysis- Breaking down a polymer
  • Requires a water molecule
four main classes
Four Main Classes
  • Carbohydrates
  • Lipids
  • Proteins
  • Nucleic Acids
carbohydrates
Carbohydrates
  • Sugars and their related compounds
  • Oxygen and Hydrogen in a 1:2 ratio
  • Energy stores or structure
  • Most end in -ose
monosaccharide
Monosaccharide
  • Simple Sugars
  • Contain 3, 4, 5, or 6 carbon atoms
monosaccharide1
Monosaccharide
  • Deoxyribose
    • Five carbons
    • In Nucleic Acids
  • Glucose
    • Six carbons
    • Energy
disaccharides
Disaccharides
  • Two monosaccharides
  • Ex. lactose and sucrose
polysaccharide
Polysaccharide
  • Glycogen- Energy storage in animals
  • Starch- Energy storage in plants
  • Cellulose- Cell walls in plants
  • Chitin- Amino Sugars used in exoskeletons
polysaccharides
Polysaccharides
  • Polymers made of monosaccharides
lipids
Lipids
  • Nonpolar
  • Mostly carbon and hydrogen
  • Excellent in storing energy
  • Also used in membranes and waterproof surfaces
fatty acids
Fatty Acids
  • Saturated
  • Monounsaturated
  • Polyunsaturated
triglycerides
Triglycerides
  • Three Fatty Acids PLUS One Glycerol
  • Fats- have mostly saturated fatty acids (can be packed closer, so they are solid)
  • Oils- Unsaturated fatty acids (kinks make them liquid)
slide63
Wax
  • One long fatty acid connected to one long alcohol
  • Waterproof
steroids
Steroids

?

  • Some Hormones
  • In Cell Membranes
phospholipids
Phospholipids
  • Two Fatty Acid Tails AND One Phosphate Group
phospolipids
Phospolipids
  • Tails- Hydrophobic (water hating)
  • Head- Hydrophilic (water loving)
nucleic acids
Nucleic Acids
  • DNA and RNA
  • Made of nucleotides
    • Pentose sugar
    • Phosphate group
    • Nitrogen base (A, T, G, C, U)
nitrogen bases
Nitrogen Bases
  • Purines (2 rings): Adenine and Guanine
  • Pyrimidines (1 ring): Cytosine, Thymine, Uracil
nucleotides
Nucleotides
  • Also act as coenzymes
  • ATP, GTP
proteins2
Proteins
  • More than 50% of the dry weight of an organism
  • Made of amino acids
amino acids1
Amino Acids
  • Amino Group
  • Carboxyl Group
  • Hydrogen Atom
  • R group (20 different)
proteins3
Proteins
  • Amino Acids connected by Peptide Bonds
  • Dipeptide
  • Polypeptide
protein structure3
Protein Structure
  • Primary- Chain of amino acids
  • Secondary- Due to H-Bonds between amino acids
protein structure4
Protein Structure
  • Tertiary- “Active” Shape
    • H-Bonds between R-groups
    • Ionic Bonds between R- groups
    • Nonpolarity (pushed together by water)
    • Sulfur bridges (covalent bond between 2 cysteines)
    • Van der waals attractions
protein structure5
Protein Structure
  • Quarternary Structure
    • Joining of two or more polypeptide chains
groups3
Groups
  • Catalysts- Enzymes
  • Structural- for support; hair, silk, connective tissue
  • Storage- source of amino acids for young
groups4
Groups
  • Transport- of other substances
  • Hormonal- coordinates and directs regulation of organisms
  • Receptors- decide what comes in/out of cells
groups5
Groups
  • Transcription factors- tells cells what to make
  • Motor- make up muscles, cilia, flagella, etc
  • Defensive- antibodies
enzymes1
Enzymes
  • Organic Catalysts
  • Lower Activation Energy
  • May need a coenzyme in order to function
inhibition
Inhibition
  • Competitive- fight for the active site
inhibition1
Inhibition
  • Noncompetitive- inhibitor binds somewhere else (allosteric site)
    • Allosteric Enzyme- active site changes
slide90
Why?
  • Control Metabolism
  • Feedback
  • On/Off Switches