Download - THE BIOMOLECULES
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THE BIOMOLECULES Life’s Construc/on Materials
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Carbohydrates Lipids (Fats) Proteins Nucleic Acids (DNA, RNA)
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Organic Compounds (biomolecules))
• Compounds that contain carbon
• Hydrogen, oxygen, nitrogen, phosphorus and sulfur can also be found in organic compounds
A lipid (a.k.a. fat)
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Why Carbon?
• Carbon can form more bonds than any other element (4)
• This property allows carbon based molecules to be quite large and diverse
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C C Single Bond (one pair of e- shared)
C C Double Bond (2 pairs of e- shared)
C C Triple Bond (3 pairs of e- shared)
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Monomers and Polymers
Organic compounds are made of monomers - individual subunits
Many monomers form polymers - larger molecules
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Condensa/on and Hydrolysis Reac/ons
• Hydrolysis reac/ons break large molecules (polymers) into smaller ones by adding water
• CondensaEon, or dehydraEon synthesis builds large molecules from smaller ones by removing water
Two amino acids are shown at the top. In condensa/on, the amino acids are combined into a dipep/de. In hydrolysis, the dipep/de is split into two amino acids again.
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Monosaccharides (glucose, fructose, galactose)
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Condensa/on Reac/on (forming maltose – a disaccharide)
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Polysaccharides (starch vs. cellulose)
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Glycerol (monomer)
3 Fatty acids (monomers) Lipid (polymer)
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Saturated and Unsaturated FaNy Acids
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DNA (Nucleic Acid polymer)
Nucleotides (monomers)
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Nucleo/de
Five carbon sugar
Nitrogen base Phosphate group
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Two amino acids bonded together (dipeptide)
Amino acid (monomer) Amino acid (monomer)
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Protein Structure
• Proteins are polymers made of amino acid monomers
• The shape of a protein determines its func/on
• The shape is determined by the order of amino acids in the protein
p53 tumor suppressor protein
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Structure of an Amino Acid
hNp://cornellbiochem.wikispaces.com/23.2
Alpha carbon
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Four Levels of Protein Structure
• Primary‐ arrangement of amino acids in a polypep/de chain
• Secondary – forma/on of por/ons of the amino acid chain into alpha helices or beta‐pleated sheets
• TerEary – folding of whole polypep/de chain into a 3‐D structure (due to interac/ons of R‐groups of amino acids in the chain)
• Quaternary – aNrac/ons between more than one polypep/de chain (results in a larger func/onal protein)
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Enzymes • Proteins that regulate chemical reac/ons in an organism
• Enzymes speed up the rate of chemical reac/ons
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Chemical Reac/ons
reactants products
C6H12O6 + 6 O2 6 CO2 + 6 H2O (cellular respiration)
The atoms of the reactants are rearranged to form products.
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Enzymes act as Catalysts
Catalysts speed up chemical reactions without being used up or changed during
the reaction
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How do Enzymes Speed up Chemical ReacEons?
• The energy required to get a chemical reac/on started is the ac#va#on energy
• Enzymes work by lowering the ac.va.on energy of a given reac/on to speed up the reac/on
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Specificity
• Every enzyme acts on a substrate
• The acEve site is the area where the enzyme modifies the substrate
• Induced fit – substrate binds to enzyme cause enzyme to “mold” around the substrate (conforma/onal change)
hNp://www.websters‐online‐dic/onary.org/defini/ons/Enzyme?cx=partner‐pub‐0939450753529744%3Av0qd01‐tdlq&cof=FORID%3A9&ie=UTF‐8&q=Enzyme&sa=Search#922
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Factors affec/ng the rate of an enzyme catalyzed reac/on
• Amount of enzyme present
• Amount of substrate present
• Temperature and pH
• Inhibitors
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Inhibitors (compe//ve vs. noncompe//ve)
• Compe//ve inhibitors bind at the ac/ve site of the enzyme
• Noncompe//ve inhibitors don’t bind at the ac/ve site, but cause a conforma/onal change in the ac/ve site
• Both slow down reac/on rate of the enzyme Compe//ve vs. noncompe//ve
inhibi/on
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Enzyme Denatura/on Enzyme is shown in yellow Blue molecules are the substrate
Heat or pH change
Reac/on takes place normally
No reac/on occurs (ac/ve site is damaged and substrate no longer fits)