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Indietro

Unit 1 vocabs

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  • Properties of water (9~)


    • Polarity

    • Cohesion

    • Adhesion

    • Capillary action

    • High specific heat

    • High heat of vaporization

    • Density (ice is less dense than water)

    • Universal solvent (both an acid and a base bc it can gives an H+ or OH-)

    • Neutral pH & it's a buffer (can resist change in pH)

  • Functional group: Hydroxyl


    -OH

  • Functional group: Carbonyl


    -C=O

  • Functional group: Carboxyl


    -COOH

  • Functional group: Amino group


    -NH2

  • Functional group: Sulfhydryl


    -SH

  • Functional group: Methyl


    CH3

  • Functional group: Phosphate group


    -\(OP3^{-2}\)

  • Formula: Dehydration synthesis (purpose)


    Formula: A + B \(\rightarrow\) AB + H2O

    • bond 2 monomers together by removing an H+ & OH- from each monomer (together form H2O)

  • Formula: Hydrolysis


    Formula: AB + H2O \(\rightarrow\)A + B

    • Break the bond of a polymer by adding an H2O

  • Macromolecule: Carbohydrate


    • Made from Carbon, Hydrogen, Oxygen

    • Monomer: Monosaccharide (CH2O)

    • Polymer: Polysaccharide

    • Bond between monomers: glycosidic linkage

  • Miscellaneous:

    1. Monosaccharides

    2. Disaccharides

    3. Polysaccharides


    1. Most common monosaccharide is glucose (nutrient use for cellular respiration)

    2. Most common disaccharide is sucrose

    3. Functions of polysaccharide:

      • Storage polysaccharide: plant store Starch & animals store Glycogen

      • Structural polysaccharide: Cellulose (plant) & Chitin (arthropod's exoskeleton)

  • Macromolecule: Lipid


    • Made from Carbon, Hydrogen, Oxygen, Phosphorous

    • Monomer: Glycerol & Fatty acids

    • Polymer: N/A

    • Bonds between monomers: ester linkage

    • Lipids are non-polar \(\rightarrow\)hydrophobic

  • Lipid: fat


    • Function:

      • Provide Energy, support cell functions, provide insulation

    • Components: glycerol & fatty acid joined by an ester linkage

  • Lipid: Saturated fat vs. Unsaturated fat


    • Saturated fat: have no double bonds in the carbon chain

      \(\rightarrow\)More Hydrogen \(\rightarrow\)Straight \(\rightarrow\) Solid at room temp

    • Unsaturated fat: have 1+ double bonds

      \(\rightarrow\)bent \(\rightarrow\)harder to pack together \(\rightarrow\) liquid at room temp

  • Lipid: Phospholipid


    • Function: major component of cell membranes

    • Component: glycerol/phosphate head + 2 fatty acid (sat & unsat)

    • Assemble as a bilayer in H2O: hydrophilic head (phosphate) and hydrophobic tails (fat)

  • Lipid:

    1. Cholesterol

    2. Steroids


    1. Cholesterol provides structural stability to animal cells

    2. Steroid:

      • Components: 4 fused rings

      • Function: unique function groups attached to rings determines the function

  • Macromolecule: Nucleic Acid


    • Made from Carbon, Hydrogen, Oxygen, Phosphorous, Nitrogen

    • Monomer: Nucleotides

    • Polymer: DNA, RNA

    • Bond: Phosphodiester linkage

  • DNA vs. RNA


    • DNA: 2 strands, deoxyribose sugar, use Thymine to bond to Adenine

      • Antiparallel (5' end (phosphate) is the opposite of 3' end (Hydroxyl end))

    • RNA: 1 strand, ribose sugar, use Uracil to bond to Adenine

  • Pyrimidines vs. Purines


    Pyrimidines: one ring w/ 6 atoms

    • Thymine (DNA)

    • Uracil (RNA)

    • Cytosine

    Purines: one ring with 6 atoms bonded to another with 5 atoms

    • Adenine

    • Guanine

  • Macromolecule: Protein


    • Made from Carbon, Hydrogen, Oxygen, Nitrogen, Sulfur

    • Monomer: Animo acid

    • Polymer: polypeptide

    • Bond: peptide bond

  • Protein : Side chain groups


    • Polar \(\rightarrow\)hydrophilic

    • Ionic/charged \(\rightarrow\)hydrophilic

    • Non-polar\(\rightarrow\)hydrophobic

  • Protein: formation of a peptide bond


    Amino group (-NH2) and Carboxyl group (-COOH) next to each other + dehydration synthesis \(\rightarrow\)peptide bond.

  • Protein: levels of protein structure


    • Primary: linear chain of AA

    • Secondary: coils & folds due to H bonds in the polypeptide backbone

      • \(\beta\)pleated sheet: folds to H bonds side by side

      • \(\alpha\) helix: coils due to H bonds every 4th AA

    • Tertiary: 3D folding due to side chain interactions

    • Quaternary: association of 2+ polypeptides chains

  • Protein: Disulfide bridges


    Covalent bond between 2 sulfur atoms of 2 cysteine molecules

    primary affect tertiary level protein bonding (3D folding)

  • Protein: functions & purpose


    • Antibody: protect against diseases & infections

    • Enzyme: speed up rxns by acting as a catalyst

    • Messenger: transmit hormones (signals)

    • Provide structure & support

    • Transport/storage: bind to small molecules to contain and carry them across the body