Building Blocks of Life # 7

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46 Terms

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Carbon

  • the central component of organic chemistry

    • all living organisms on earth are carbon based

    • all of the biomolecules that form our cells are composed of a carbon skeleton

    • a carbon atom can form 4 covalent bonds

      • each carbon atom can act as an intersection point from which a molecule can branch off in as many as four directions

        • this allows each of its bonds to rotate freely

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Form & function

  • the form (shape) and chemical structure of most organic molecules have a significant effect on how they function

    • even slight changes in chemical composition can lead to the entire molecule not functioning properly, or at all

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Isomers

  • molecules that have the same chemical formula (except same atoms) but have different structures

    • structural

    • cis-trans

    • enantiomers

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Structural isomers 

  • isomers where the arrangement of atoms in the molecule differs

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Cis-Trans Isomers

  • isomers that include a double covalent bond (have diff arrangements of atoms on either side of the bond)

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Enantiomer isomers

  • isomers that are mirror images of each other

    • chiral isomers: come in left-handed and right-handed forms

    • left is homochiral (it can only use on type of isomer)

      • all life uses only left-handed amino acids and right handed nucleic acids

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polymers

  • long chains of component molecules called monomers, connected with covalent bonds 

    • most organic molecules are polymers

    • proteins, nucleic acids, carbohydrates, lipids

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Monomers

  • amino acids, nucleotides, monosaccharides, fatty acids

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monosaccarides

  • sugar monomer

    • glucose

    • fructose

    • galactose

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proteins 

  • machinery that runs cells, provides structural support, & acts as catalysts that facilitate chemical reactions 

  • monomer: amino acids

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nucleic acids

  • encode and transmit genetic information

  • monomer: nucleotides 

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carbohydrates

  • provide source of energy and make up the cell wall in bacteria, plants, and algae

  • monomer: monosaccharides

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lipids

  • make up cell membranes, store energy, and act as signaling molecules 

  • monomer: fatty acid

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Dehydration synthesis (condensation reaction)

  • joining reaction (that chains monomers together into polymers — overall called polymerization)

    • water molecules are created each time a monomer is added to the polymer chain

    • requires energy — our cells use special proteins called enzymes to facilitate chemical reactions and make it require less energy

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Hydrolysis reaction

  • breaking reaction (that breaks a polymer apart back into its monomers)

  • to break a polymer back into monomers, a water molecule is consumed by the reaction (water molecule added back into the polymer chain and breaks a bond apart) 

  • requires energy — our cells use special proteins called enzymes to facilitate chemical reactions and make it require less energy  

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proteins 

  • polymers, made up of individual amino acid monomers 

  • its structure/shape determines its function:

    • primary, secondary, tertiary, quaternary

  • contains a:

    • carboxyl group, phosphate group, amino group, r-group, peptide bond

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carboxyl groups

  • inside of proteins 

  • C, O, OH

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Amino groups

  • inside proteins

  • H2N

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R-groups

  • R

  • causes protein to fold under certain circumstances

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Peptide bond

  • the bond created between the amino group and the carboxyl group when the dehydration synthesis reaction joins the two (takes out the OH and the H and replaces it with a bond)

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primary, secondary, tertiary, and quaternary

list the 4 different protein structures/shapes

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primary protein structure

  • the linear chain of covalent peptide bonds

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secondary protein structure 

  • twisted chain of amino acids that form hydrogen bonds between the amino and carboxyl groups (single Helix) 

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tertiary protein structure

  • 3D folding of a protein, determined by the r-groups

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hydrophobic r-groups

  • cause the protein to fold into itself to avoid water

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hydrophilic r-groups

  • cause hydrogen bonds to form between folds, strengthening the structure

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quaternary protein structure

  • a protein, composed of smaller proteins (subunits)

  • ex) hemoglobin

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proteins

  • roles:

    • catalyse reactions

    • defend / protect the cell

    • nutrient storage and transfer

    • transport - move other molecules

    • hormonal - bodily function coordination

    • receptor / detect & react

    • movement

    • structural / support

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DNA (deoxyribonucleic acid)

  • nucleic acid polymer

  • composed of deoxyribonucleotides (nucleotide monomer)

  • double stranded = double helix

  • contains deoxyribose sugar

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RNA (ribonucleic acid) 

  • nucleic acid polymer 

  • composed of ribonucleotides (nucleotide monomer) 

  • single stranded 

  • contains ribose sugar 

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purines (nucleobases)

  • Adenine (A)

  • Guanine (G)

  • have a double ring structure

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pyrimidines (nucleobases) 

  • uracil (U)

  • thymine (T) 

  • cytosine (C)

  • have a single ring structure 

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phosphodiester bond

  • the kind of bond that links together nucleotides to form nucleic acid polymers

    • the phosphate group attaches to the 5’ carbon, covalently bonds with the 3; carbon through dehydration synthesis

    • these bonds makeup the backbone of nucleic acids and make the polymer resilient against heat and pH

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carbohydrates 

  • the fuel that keeps cells running (one of the major energy storage biomolecules) 

  • these polymers can also be used for structural integrity at multiple levels

  • 3 levels of complexity:

    • disaccharides, polysaccharides, glycosidic bond

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disaccharides

  • two monomers chemically bound together in a single compound

    • when two monosaccharides are linked by a glycosidic bond they form a ______

    • sucrose (glucose + fructose)

    • lactose (glucose + galactose)

    • maltose (glucose + glucose)

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polysaccharides

  • three or more monomers chemically bound into a single compound

    • many monosaccharides in various combinations and orientations

    • two primary functions:

      • energy storage

      • structural support

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glycosidic bond

  • covalent bonds that link monosaccharides together 

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Lipids

  • defined by a shared property (they are partially or completely hydrophobic) - nonpolar

  • not made from repeating monomers

  • not defined by a structure

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neutral fats

  • used for energy storage, insulation from cold, protection of internal organs

    • made up of fatty acid molecules and glycerol molecules

    • # of fatty acids per glycerol range from 1-3

      • 1=monoglyceride

      • 2=diglyceride

      • 3=triglyceride

      • * fatty acids can be saturated or unsaturated)

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phospholipids 

  • major constituents of our cell membranes 

  • 1 glycerol, 1 phosphate group, 2 fatty acid chains

  • are amphipathic 

  • when exposed to water they self assemble into a bi-layer, that sheilds the hydrophobic tails from the water (hydrophobic tails on inside)

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amphipathic

  • have a hydrophilic head & a hydrophobic tail

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steroids

  • maintain the fluidity of cell membranes & signal molecules

    • based on sterol: 4 fused rings composed of 20 bonded carbon atoms

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glycerol

  • bonds with fatty acids via an ester bond

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ester bond

  • bonds together glycerol and fatty acids

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saturated fatty acids

  • all carbon atoms in the hydrocarbon chain are connected to each other by single covalent bonds

    • remainder of carbon bonds have an attached hydrogen

      • molecule is saturated with hydrogen

    • solid @ room temp

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unsaturated fatty acids 

  • when some of the carbon atoms in the hydrocarbon chain are linked by double covalent bonds 

    • missing some hydrogen atoms

      • not saturated with hydrogen

    • double bond = “kink” in the molecule, prevents molecules from stacking on top of each other

    • can occur in Cis or Trans isomers

      • trans-fats = not good for you