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1.2: Biologically Important Macromolecules

McGraw Hill Section 1.2

Ms. Klodt

on 18 January 2018

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Transcript of 1.2: Biologically Important Macromolecules

Biologically Important

Fatty Acid
Lipid bilayer
Amino acid
Nucleic acid
Key Terms
Macromolecules are large, complex molecules
mers - chain like molecules made of smaller molecules joined by covalent bonds
mers - smaller molecules that make up a polymer
Types of Biological Molecules
Energy storage but easily broken down
Always contain C, H, and O
General formula is CH2O
Mostly polar and hydrophilic
Long term energy storage
Insulation, cushion, cell membrane
Mono & Disaccharides
Monosaccharides have between 3-7 sugar molecules joined together
Glucose, Fructose, Galactose
isomers - molecules with the same molecular formula (C6H12O6) but different structures
Disaccharides are made of 2 monosaccharides joined together
The covalent bond joining them is called a glycosidic linkage
Lactose = Glucose + Galactose
Made of monosaccharides joined together
Differences in linkages result in different biological uses
Glycogen, Starch, Cellulose
Made of a glycerol molecule and 3 fatty acid molecules
Joined with bonds called ester linkages
Fatty acids are hydrocarbon chains that end with a -COOH group
Saturated fatty acids: only single bonds
Unsaturated fatty acids: One or more double bonds
One double bond: Monounsaturated
Two or more: Polyunsaturated
Hydrogenation: adding hydrogens to unsaturated fats to produce saturated fats
Cell membranes
2 Fatty acid tails attached to a glycerol, which is attached to a phosphate group. Attached to that group is another group of atoms
The fatty acid tails are hydrophobic, while the rest are hydrophilic
This allows for a lipid bilayer, with the tails facing in, and the heads facing out into water
Made of 4 carbon rings attached to each other
Includes cholesterol, testosterone and estrogen
Made by plants and animals
Solid at room temperature
Coat and repel water
Other Lipids
Diverse group of macromolecules, defined by function
Enzymes & catalysts
Structure - hair, nails, claws, etc.
Regulation of cell processes
Immune functions
molecules containing a hydrogen atom, an amino group, a carboxyl group and a side chain (or R group)
The side chains determine function
Essential amino acids cannot be created by the body and must be consumed
Bonds between amino acids are called peptide bonds
formed between the carboxyl group on one and the amino group on another
A polymer of amino acids is called a polypeptide. Multiple polypeptides make a protein.
Amino Acids
Amino Acids
There are four levels of organization
Primary Structure: Linear sequence of amino acids
Peptide bonds between amino acids form the backbone
Hydrogen bonds form between the C=O and N-H of different amino acids
Secondary Structure: Pleated or helix structure
Tertiary Structure: Complex, 3D folding forming a protein
Quaternary Structure: Multiple Tertiary Structures joined together
Denaturation is when proteins unfold, due to breaking of intramolecular bonds. This destroys the protein.
Caused by extreme temperatures and pH imbalances
Protein Organization
Nucleic Acids
Two kinds
Deoxyribonucleic Acid (DNA)
Contains genetic material
Turned into proteins
Ribonucleic Acid (RNA)
Assists in conversion of DNA to protein
Composed of nucleotide polymers
Nucleotides are made of a phosphate group, a 5 carbon sugar (deoxyribose or ribose) and a nitrogenous base (DNA: Adenine, thymine, guanine and cytosine. RNA: Thymine is replaced with uracil)
Bonds between nucleotides is called phosphoidester bond, between phosphate on nucleotide and hydroxyl on the next
DNA resembles a ladder, with the uprights being made of the sugar and phosphate groups, and the rungs being the nitrogenous bases
Thymine (or uracil) always pairs with adenine and guanine with cytosine
Nucleic Acid Structure
Full transcript