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Biochemistry
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Organic Molecules Molecules that have a carbon skeleton and covalent carbon-hydrogen bonds Can be man made
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Carbon Can form 4 covalent bonds
Allows for molecular diversity in shape and length
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Miller/Urey Experiment
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Review of Functional Groups
ID the various functional groups in the following molecules…
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Phosphate Adenosine
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Carboxyl group (COOH) It’s a fatty acid… why acid?
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Ethanol… alcohol in adult beverages
OH… looks like ____... Alcohol can make you do these types of things…
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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.
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Aldehyde Think… formaldehyde stinks… put it on the end! Ketone trick?
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Proteins More than 50% of the dry weight of an organism
Made of smaller subunits (monomers) amino acids
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Amino Acids Amino Group Carboxyl Group Hydrogen Atom
R group (20 different different properties)
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Proteins Amino Acids connected by Peptide Bonds Dipeptide Polypeptide
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Protein Structure (a) A ribbon model Groove Figure 5.19
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Protein Structure Primary- Chain of amino acids
Secondary- Due to H-Bonds between amino acids
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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
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Protein Structure Quarternary Structure
Joining of two or more polypeptide chains
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(a) A ribbon model Groove Figure 5.19
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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)
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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?
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Fig. 5.1 Shows all the functions proteins can have:
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Groups Catalysts- Enzymes speed up rates of chem. rxns
Structural- for support; hair, silk, connective tissue Storage- source of amino acids for young
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Groups Transport- of other substances
Hormonal- coordinates and directs regulation of organisms Receptors- decide what comes in/out of cells
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Groups Transcription factors- tells cells what to make
Motor- make up muscles, cilia, flagella, etc Defensive- antibodies
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Enzymes Organic Catalysts Lower Activation Energy
May need a coenzyme in order to function
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Factors affecting enzymes
Do the Lab!!!
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Isomers Isomers- Molecules with same atoms but different arrangement and properties
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Functional Groups Groups of atoms that give a molecule specific properties
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Hydroxyl Alcohols
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Carbonyl Ketones, formaldehyde
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Carboxyl “Organic” Acids
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Amino Amino Acids
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Sulfhydryl Found in proteins
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Phosphate Phospholipids, Nucleotides OR
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Building Macromolecules
Monomers- Small organic molecules that can be linked together Polymers- Big things (monomers linked together)
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Building Condensation (dehydration synthesis): connects 2 molecules.
One molecule loses an H, the other loses an OH One water molecule is formed
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Taking Apart Hydrolysis- Breaking down a polymer Requires a water molecule
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Four Main Classes Carbohydrates Lipids Proteins Nucleic Acids
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Carbohydrates Sugars and their related compounds Oxygen and Hydrogen in a 1:2 ratio Energy stores or structure Most end in -ose
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Monosaccharide Simple Sugars Contain 3, 4, 5, or 6 carbon atoms
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Monosaccharide Deoxyribose Five carbons In Nucleic Acids Glucose
Six carbons Energy
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Disaccharides Two monosaccharides Ex. lactose and sucrose
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Polysaccharide Glycogen- Energy storage in animals
Starch- Energy storage in plants Cellulose- Cell walls in plants Chitin- Amino Sugars used in exoskeletons
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Polysaccharides Polymers made of monosaccharides
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Lipids Nonpolar Mostly carbon and hydrogen Excellent in storing energy Also used in membranes and waterproof surfaces
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Fatty Acids Saturated Monounsaturated Polyunsaturated
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Three Fatty Acids PLUS One Glycerol
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)
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Triglycerides
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Wax One long fatty acid connected to one long alcohol Waterproof
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Steroids ? Some Hormones In Cell Membranes
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Phospholipids Two Fatty Acid Tails AND One Phosphate Group
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Phospolipids Tails- Hydrophobic (water hating)
Head- Hydrophilic (water loving)
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DNA and RNA Made of nucleotides Pentose sugar Phosphate group
Nucleic Acids DNA and RNA Made of nucleotides Pentose sugar Phosphate group Nitrogen base (A, T, G, C, U)
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Nitrogen Bases Purines (2 rings): Adenine and Guanine Pyrimidines (1 ring): Cytosine, Thymine, Uracil
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Nucleotides Also act as coenzymes ATP, GTP
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Proteins More than 50% of the dry weight of an organism
Made of amino acids
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Amino Acids Amino Group Carboxyl Group Hydrogen Atom
R group (20 different)
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Proteins Amino Acids connected by Peptide Bonds Dipeptide Polypeptide
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Protein Structure Primary- Chain of amino acids
Secondary- Due to H-Bonds between amino acids
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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
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Protein Structure Quarternary Structure
Joining of two or more polypeptide chains
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Groups Catalysts- Enzymes
Structural- for support; hair, silk, connective tissue Storage- source of amino acids for young
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Groups Transport- of other substances
Hormonal- coordinates and directs regulation of organisms Receptors- decide what comes in/out of cells
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Groups Transcription factors- tells cells what to make
Motor- make up muscles, cilia, flagella, etc Defensive- antibodies
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Enzymes Organic Catalysts Lower Activation Energy
May need a coenzyme in order to function
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Factors affecting enzymes
Do the Lab!!!
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Inhibition Competitive- fight for the active site
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Inhibition Noncompetitive- inhibitor binds somewhere else (allosteric site) Allosteric Enzyme- active site changes
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Why? Control Metabolism Feedback On/Off Switches
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