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Module
9 (NINE)
Module
10 (TEN)
100

Identify classes of organic compounds that contain sulfur.

  • Derivatives of hydrogen sulfide (H-S-H)

    • Thiol (Thi means sulfur) (Like alcohol)

      • C-S-H

    • Sulfide (Like ether)

      • C-S-C

    • Disulfide

      • C-S-S-C

    • Thioester (Like ester)

      • O=C-S-C

100

Identify physical properties of organic compounds that contain nitrogen.

  • Makes 3 bonds

  • Can have 4 covalent bonds if they have a positive charge

  • Pungent smell, similar to ammonia

100

Identify alkaloids, neurotransmitters and related amines.

  • Alkaloids:

    • Nitrogen-containing

    • Alkaline (basic compounds)

    • Obtained from plants

    • End in -ine


  • Consumer products: Nicotine, caffeine 

  • Poisons: Coniine, atropine

  • Pain killers: Morphine, codeine, heroin


  • Neurotransmitters:

    • Norepinephrine

    • Dopamine

    • Serotonin

    • Acetylcholine


  • Related amines:

    • Epinephrine

    • Amphetamine

    • N-Methylamphetamine

100

Distinguish amino acids, dipeptides, polypeptides and proteins.

  • Amino acids:

    • Building block/monomer

    • Builds proteins

    • 20 amino acids

  • Dipeptides:

    • 2 linked amino acids

    • Tripeptide = 3 linked amino acids

  • Polypeptides:

    • Many linked amino acids (3-49)

    • Polymer

  • Proteins:

    • 50+ amino acids linked together

    • Very large molecule

100

Identify physical properties of amino acids.

  • Physical state: White solid at room temp (strong interparticle force)

  • Melting point: High (strong interparticle force)

  • Solubility in water: Soluble (depends on pH of solution) – Establish contact w/ water

  • Electrical conductivity: Solutions are electrolytes

    • Demonstrates properties of ionic compounds

200

Identify physical properties of organic compounds that contain sulfur.

Physical properties:

  • Makes 2 bonds (like oxygen)

  • Often smells bad

  • Hydrogen sulfide is emitted from rotten eggs

200

Identify the names and structures of simple amines.

  • N bonded 3 times & to a carbon at least once

  • (Primary) Same as alkanes with -amine at the end (methanamine)

200

Describe dissociation reactions of amines.

Bronsted reversible reaction:

Amine + Water reversible  alklammonium ion (NH4+) + hydroxide ion (OH-)

  • Transfer H+ from H2O to amine, to make OH-

200

Identify the importance of proteins in biology.

  • Involved in most biological activities

  • A protein is usually involved with most tasks being done inside your body

  • Help with diagnosing health problems by looking to see if they’re large, and can’t pass through membranes

  • Catalysis

  • Structure

  • Storage

  • Protection

  • Regulation

  • Nerve impulse transmission

  • Movement

  • Transport

200

Describe dehydration condensation reactions of amino acids.

Amino acid + amino acid → dipeptide + H2O

  • Condensation = linkage

  • Dehydration = losing water after linking

300

Describe oxidation reactions of thiols.

2 Thiols ⇌ 1 disulfide

Oxidation (losing electrons); needs oxidizing agent [O]

  1. Remove H from sulfhydryl group (SH) of 1 thiol

  2. Remove H from sulfhydryl group (SH) of other thiol

  3. Connect the exposed sulfur atoms by a single bond

Reduction (gaining electrons); needs reducing agent [H]

  1. Cut disulfide single bond, leaving 2 exposed sulfur atoms

  2. Attach H atom to one, making sulfhydryl group

  3. Attach H atom to other, making sulfhydryl group

300

Classify amines.

  • 1 - Primary: NH2 group: Nitrogen directly attached to 1 Carbon

  • 2 - Secondary: Nitrogen directly attached to 2 carbons

  • 3 - Tertiary: 3 carbons

300

Describe neutralization reactions of amines.

Do neutralization reactions w/ strong acids (one way arrow)

  • Not reversible

Amine + Acid → alkylammonium ion (NH4+) + Cl-

Becomes an amine salt NH4+Cl- after boiling out water from aqueous solutions

300

Classify proteins (simple, conjugated, fibrous, globular, complete, incomplete).

Nutrition:

  • Complete: Has all 20 amino acids, usually come from animals

  • Incomplete: Is missing 1 or more essential amino acids, usually come from plants


Composition:

  • Simple: Only have amino acids, no prosthetic groups

  • Conjugated: Crumpled up piece of paper

    • Made up of amino acids & prosthetic groups (nucleic acids, lipids, carbs, phosphate group, heme, iron, metals)


    Shape; have secondary Components:

  • Fibrous: Elongated

    • Water insoluble

    • Contain long stretches of either Alpha-Helix or Beta-Sheet segments


  • Globular: Segments of Alpha-Helixes, B-Sheets, & random coils

    • Includes secondary &/or tertiary interactions

    • Water soluble

300

Describe the primary structure of proteins.

Order of amino acids from one end of a protein to the other

  • Sequence/list

  • Determines shape of protein, which determines function of proteins

  • Not affected by denaturation

400

Describe reactions of thiols with heavy metal ions.

2 Thiols → Disulfide-metal complex

  1. Take off hydrogrens from thiols

  2. Put heavy metal ion in between both of the exposed sulfur atoms

400

Identify heterocyclic amines.

Ring compounds w/ at least 1 corner nitrogen in cyclic ring structure

  • Must show nitrogen in corners

400

Describe the structure and solubility of amine salts.

  • Similar to table salt

  • High MP

  • Soluble in water

  • Ionic

400

Identify amino acid structure and classify amino acid side chains.

  • Neutral/nonpolar: Mostly hydrocarbons, sulfide, thiol

  • Neutral/polar: Alcohols, phenols, amides

  • Acidic: Carboxylic acid → Carboxylate ions (-COO-)

  • Basic: Amines, double bonded nitrogens → cations +

400

Describe the secondary structure of proteins.

Backbones of proteins contain useful N-H bonds & O atoms

  • Hydrogen bonding of N-H bonds & O atoms stabilizes structure

  • Fold to give 2 types of secondary structures:

    • Alpha-Helix: Helical shape (DNA)

    • Beta-Pleated Sheet: Looks like paper folded in fan shape

  • Random coil:

  • Segments where backbone doesn’t make a helix or sheet

500

Identify classes of organic compounds that contain nitrogen.

  • Amine (-N-C)

  • Amide (O=N-C)

  • Amino group (NH2)

500

Classify amides.

  • Have a carbonyl group attached to a nitrogen

  • Simple: Nitrogen attached to 1 carbon & 2 hydrogens

  • Monosubstituted: Replace a hydrogen with a carbon extension (2 carbons)

  • Disubstituted: Replace both hydrogens with a carbon extension (3 carbons)

500

Identify the structural similarities between esters and amides.

  • They both link smaller molecules together

  • Don’t react w/ water

  • pH stays same

500

Define and identify stereoisomers, chiral carbons and enantiomers.

  • Steroisomers: Isomers with attached atoms or groups arranged differently in a molecule

  • Chiral carbons: One carb attached to 4 different atoms

  • Enantiomers: Have different arrangements around a tetrahedral carbon (mirror images)

500

Describe the tertiary structure of proteins.

  • After backbone orders itself into secondary structure

  • Focuses on side chains

  • Connects remote parts of 1 protein chain

  • Side chains associate by:

    • Disulfide bridge (S-S bond)

      • Oxidizing 2 thiols → disulfide

      • Knock off H’s and connect S-S

  • Salt bridge (COO- * * * * H3N+ bond)

    • Connect negative & positive charges together

    • Ionic bonding

  • Hydrophobic interactions (Benzyne-Benzyne or CH-CH interactions)

    • Aromatic rings

    • Nonpolar structures interacting

  • Hydrogen bonding (Hydrogen of H-O, H-N, H-F connected to O, F, N)