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Lecture 3

BIOL 1201 Lecture Notes - Lecture 3: Carboxylic Acid, Dehydration Reaction, Glycerol

Biological Sciences
Course Code
BIOL 1201
E William Wischusen

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a.Organic molecules
a. Complex molecules containing a carbon-carbon bond
b. Composed largely of C, H, O, N (S,P)
c. Classes
a.i. Carbohydrates
a.i.1. Compounds with a ratio of
a.i.1.a. CH2O
a.i.1.a.i. 1:2:1 ratio
a.i.2. Monosaccharides
a.i.1.a. 1 carbon sugar
a.i.1.b. Every 2 makes 1 polymer
a.i.2. Disaccharides
a.i.1.a. 2 sugars
a.i.1.b. Processed through condensation reaction
a.i.1.a.i. Produces water
a.i.1.b. Dehydration synthesis
a.i.1.a.i. Removes water
a.i.1.b. Hydrolysis
a.i.1.a.i. Adds water to break down polymer
a.i.2. Polysaccharides
a.i.1.a. Many sugars
a.i.1.b. Cellulose
a.i.1.a.i. Structural
a.i.1.b. Starch
a.i.1.a.i. Storage (plants)
a.i.1.b. Glycogen
a.i.1.a.i. Storage (animals)
a.ii. Lipids
a.i.1. Insoluble in water
a.i.2. Non-polar
a.i.3. Types of Lipids
a.i.1.a. Fatty acids
a.i.1.a.i. Hydrocarbon chain with a carboxyl group on one
a.i.1.a.ii. Saturated
All the carbons are carrying max number of
hydrogen; all carbons are single bonded to each other
a.i.1.a.i. Unsaturated
Carbon Carbon double bonds, which
reduces the number of hydrogens that are carried by the
a.i.1. Triglycerides (fats)
a.i.1.a. A glycerol molecule with 3 fatty acid chains attached
a.i. Phospholipids
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a.i.1. A glycerol molecule with 2 fatty acid chains and a phosphate
group attached
a. Steroids
a.i. 4 carbon rings with various side groups
a.ii. Three 6-sided rings and one 5-sided ring.(carbon rings)
i. Proteins
a. Polymers of amino acids
b. Unbranched chains (liner molecules)
c. Amino Acids
a.a. Contains central C (carbon) to which is attached
a.b. Amino group
a.c. Carboxyl group
a.d. Hydrogen
a.e. Something else (R group)
a. Amino acid polymers
a. Amino acids are joined to form un-branched chains
a.a. The bond joining the amino acids is a Peptide Bonds
a.a.i. Results from condensation reaction
a. Protein Structure
I. Primary 1
a. A description of the covalent bonds and the sequence of amino
acids in a protein
b. Amino end to the carboxyl end
II. Secondary 2
a. Repeated spatial pattern
b. Alpha helix
c. Beta pleated sheet
d. Largely stabilized by hydrogen bonds
II. Tertiary 3
a. 3-D pattern of folding
b. Largely stabilized by weak bonds
c. Hydrogen and hydrophobic interactions
II. Quaternary 4
a. 3-D pattern joining several different polypeptide chains
b. Largely stabilized by weak bonds
c. Proteins change shape
d. Denaturation
e. Unravel of normal proteins make denatured proteins
a. Put together denatured protein to make a normal protein
b. Protein Functions
a. Structural
a.a. Muscle, cartilage, hair, feather
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b. Regulatory
a.a. Enzymes, hormones, carriers
i. Nucleic acids
a. Polymers of nucleotides
b. Unbranched chains
c. Nucleotides
a.a. 5-carbon sugar
a.b. Ribose -RNA
a.c. Deoxyribose- DNA
d. Phosphate group
a. Nitrogenous base (5types)
e. DNA structure
a. Four nucleotides
b. Complementary base Pairing (hydrogen bonds)
c. double Helix
d. Anti-parallel backbones
e. Adenosine Triphosphate
f. Not only a component of nucleic acids, but also important in cellular
I. Functional groups
a. Group of atoms attached to carbon backbone of organic molecules
b. Cause changes in physical characteristics and chemical properties
II. Hydroxyl
a. -OH
b. Polar functional group
II. Carbonyl
a. -C = O
b. Carbon with a double bond oxygen
c. Ketone located in a carbon chain
d. Aldehyde located on the end of a chain
e. Polar functional group
II. Carboxyl
a. HO - C = O
b. H+ -O - C = O turns to this when it disassociates
c. Disassociate to make an H+
d. Polar functional
e. acidic functional
f. Amino acids are acids because of the presence of the carboxyl group
g. Carboxyl group can written in the form COOH
h. Always on the end of a chain
II. Amino
a. H - N - H
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