Gen Bio I Lecture 3

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Last updated 4:19 AM on 10/1/26
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25 Terms

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Hydrocarbons

  • C and H

  • Nonpolar, hydrophobic (note: nonpolar → hydrophobic, polar → hydrophilic. to remember this, remember that water is a polar molecule so it’s hydrophillic or “water loving”)


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Functional groups


  • Hydroxyl (-OH):

  • Carbonyl (-CO)

  • Carboxyl (-COOH):

  • Methyl (-CH3):

  • Amino (-NH2):

  • Phosphate (-OPO 2/3):


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Hydroxyl (-OH):

  • Polar

  • Hydrophillic

  • Alcohol (more specific example ethanol)


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Carbonyl (-CO)

  • Polar (less than OH)

  • Hydrophillic

  • Sugars (ex. glucose)


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Carboxyl (-COOH):

  • Polar

  • Hydrophillic

  • Acidic


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Methyl (-CH3):

  • Non-polar (the only non-polar one)

  • Hydrophobic


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Amino (-NH2):

  • Polar

  • Basic

  • Hydrophillic

  • Amines (in amino acid)


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Phosphate (-OPO 2/3):

  • Polar

  • Hydrophillic

  • Acidic

  • Used in nucleic acids, ATP


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Macromolecule terms (marcomolecules, polymers, monomers)

  • Macromolecules: Large molecules made up of thousands of atoms

  • Polymers: Macromolecules made of chains of monomers

  • Monomers: Small molecules


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Two types of actions to know with molecules

  • Dehydration synthesis

  • Hydrolosis


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Dehydration synthesis

  • Making a polymer

  • Dehydration removes a water molecule forming a new bond for a polymer

  • Some enzymes that perform this are:

    • DNA polymerase: joins nucleotides together to build DNA

    • Glycogen synthase: joins glucose units to build glycogen

    • Peptide synthetases: help assemble certain peptides


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Hydrolosis

  • Opposite of dehydration synthesis

  • Adding water to break a bond

  • Enzymes that perform this are called hydrolases (not important to know but yeah)


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4 Classes of Biological Macromolecules

  • Carbohydrates

  • Lipids (note: all of these are polymers except lipids)

  • Proteins

  • Nucleic Acids


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Carbohydrates

  • Chemical formula: CH2O

  • Polymer

  • Made of C, H, O

  • Made up of monomers called monosaccharides (sugar monomers).

  • Glycosidic linkages


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What connects carbohydrates?

  • Glycosidic linkages: These monosaccharides are connected by glycosidic linkages to form polysaccharides


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Function and examples of carbohydrates

  • Function: Structure

  • IRL ex. of carbohydrates:

    • Glucose → starch = plant energy storage
      Glucose → glycogen = animal energy storage
      Glucose → cellulose = plant structure/cell walls


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Lipids

  • Hydrophobic

    • Instead dissolves in nonpolar solvents, ex. chloroform

  • Functions:

    • Storage (ex. body fat/adipose tissue)

    • Structure (ex. phospholipid bilayer)

    • Signaling (ex. hormones)

  • Lipid synthesis:

    • Dehydration synthesis & ester linkage

  • 3 types of lipids: fats, phospholipids


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Fats

  • Most abundant lipid

  • Energy storage containing 9 cal/gram (meanwhile carbs and proteins are 4 cal/gram

  • Structure: Glycerol

    • 3 carbon

    • 3 hydroxyl groups

    • note: not that important to know specific structure but do know glycerol

  • ex. meats, oils, junk food


<ul><li><p>Most abundant lipid</p></li><li><p>Energy storage containing 9 cal/gram (meanwhile carbs and proteins are 4 cal/gram</p></li><li><p>Structure: Glycerol</p><ul><li><p>3 carbon</p></li><li><p>3 hydroxyl groups</p></li><li><p>note: not that important to know specific structure but do know glycerol  </p></li></ul></li><li><p>ex. meats, oils, junk food</p></li></ul><p></p>
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<p>Phospholipids</p>

Phospholipids

  • Glycerol + 2 fatty acids + phosphate group

  • This is the head tail structure used in the phospholipid bilayer

    • Phosphate head, fatty acid tail


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Steroids

  • Has three 6 carbon rings, one 5 carbon ring

  • Ex. cholesterol, sex hormones


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Proteins

  • Polymer

  • Amino acids:

    • All amino acids have the same structure containing: central alpha carbon, hydrogen atom, amino group (basic pH), carboxyl group (acidic pH), R group

    • There are 20 types of amino acids, with each one having a different R groups


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What connects proteins?

  • Peptide bonds

  • Amino acids join together through peptide bonds

  • Amino acids joining → peptide bonds → polypeptide chain → folded protein


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Protein structure (4 levels & what they are, denaturation)

  • There are 4 levels of protein organization: primary → secondary → tertiary → quaternary structure


  • Secondary structure → small folds

  • Tertiary structure → 3D shape

  • Quaternary → Multiple polypeptide chains


  • Denaturation: A protein losing its normal shape

    • Things that can cause this are high temperatures, extreme pH, and certain chemicals

    • ex. cooking an egg making egg white clear → white


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Protein functions

  • Structure

  • Signaling/communication

  • Enzymes

  • Defense

  • Transport

  • Basically everything except heredity


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Nucleic Acids

  • DNA and RNA