AP Bio chap 5 The Structure and Function of Large Biological Molecules
Monomers | Polymers | Macromolecules |
---|---|---|
Small organic Used for building blocks of polymers, Connects with condensation reaction (dehydration synthesis) | Long molecules of monomers, With many identical or similar blocks linked by covalent bonds | Giant molecules, 2 or more polymers bonded together |
Amino acid → peptide →polypeptide → protein
smaller → larger
Dehydration Synthesis**(Condensation Reaction)** | Hydrolysis |
---|---|
Make polymers | Breakdown polymers |
Monomers → Polymers | Polymers → Monomers |
A + B → AB | AB → A + B |
_ + _ → _ + H20 | _ + H20 → _ + _ |
Writing quiz 9/20 is about proteins
“Proteios” = first or primary
50% dry weight of cells, Contains: C, H, O, N, S
Protein Functions + examples, know 4/5
Enzymes (lactase) (most end in -ase)
Defense (antibodies)
Storage (milk protein = casein)
Transport (hemoglobin)
Hormones (insulin)
Receptors - Proteins are unable to cross cell membrane
Movement (motor proteins)
Structure (keratin)
Writing quiz 9/20 vvv
Four Levels of Protein Structure
Primary
Amino acid (AA) sequence
20 different AA’s
peptide bonds link AA’s
R group = side chains
Properties:
hydrophobic
hydrophilic
ionic (acids & bases)
“amino” : -NH2
“acid” : -COOH
Please tell us how a protein comes together
Secondary
Gains 3-D shape (folds, coils) by H-bonding
Alpha (α) helix, Beta (β) pleated sheet
Basic Principles of Protein Folding
Hydrophobic AA buried in interior of protein (hydrophobic interactions)
Hydrophilic AA exposed on surface of protein (hydrogen bonds)
Acidic + Basic AA form salt bridges (ionic bonds).
Cysteines can form disulfide bonds.
Tertiary
Bonding between side chains (R groups) of amino acids
H bonds, ionic bonds, disulfide bridges, van der Waals interactions
Quaternary
2+ polypeptides bond together
9/20 primary structure to Quaternary structure
Chaperonins: assist in proper folding of proteins
Protein structure and function are sensitive to chemical and physical conditions
Unfolds or denatures if pH and temperature are not optimal
solidity (very salty) can denature
Can nature and denature naturally or can denature and never come back (faulty protein)
change in structure = change in function
Nucleic Acids - Function: store hereditary info
DNA | RNA |
---|---|
Double-stranded helix N-bases: A, G, C, Thymine Stores hereditary info Longer/larger Sugar: deoxyribose | Single-stranded N-bases: A, G, C, Uracil Carry info from DNA to ribosomes tRNA, rRNA, mRNA, RNAi Sugar: ribose |
Nucleotide = Sugar + Phosphate + Nitrogen Base
Carbohydrates
**__Fuel __**and building material
Include simple sugars (fructose) and polymers (starch)
Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O
monosaccharide → disaccharide → polysaccharide
Monosaccharides = monomers (eg. glucose, ribose)
Polysaccharides:
Storage (plants-starch, animals-glycogen)
Structure (plant-cellulose, arthropod-chitin)
Starch = α glucose monomers
Cellulose = β glucose monomers
Lipids
Fats (triglyceride): store energy
Glycerol + 3 Fatty Acids
saturated, unsaturated, polyunsaturated
Steroids: cholesterol and hormones
Phospholipids: lipid bilayer of cell membrane
hydrophilic head, hydrophobic tails
Saturated | Unsaturated / Polyunsaturated |
---|---|
“saturated” with H | Have some C=C, result in kinks |
In animals | In plants |
Solid at room temp. | Liquid at room temp. |
Eg. butter, lard | Eg. corn oil, olive oil |
Monomers | Polymers | Macromolecules |
---|---|---|
Small organic Used for building blocks of polymers, Connects with condensation reaction (dehydration synthesis) | Long molecules of monomers, With many identical or similar blocks linked by covalent bonds | Giant molecules, 2 or more polymers bonded together |
Amino acid → peptide →polypeptide → protein
smaller → larger
Dehydration Synthesis**(Condensation Reaction)** | Hydrolysis |
---|---|
Make polymers | Breakdown polymers |
Monomers → Polymers | Polymers → Monomers |
A + B → AB | AB → A + B |
_ + _ → _ + H20 | _ + H20 → _ + _ |
Writing quiz 9/20 is about proteins
“Proteios” = first or primary
50% dry weight of cells, Contains: C, H, O, N, S
Protein Functions + examples, know 4/5
Enzymes (lactase) (most end in -ase)
Defense (antibodies)
Storage (milk protein = casein)
Transport (hemoglobin)
Hormones (insulin)
Receptors - Proteins are unable to cross cell membrane
Movement (motor proteins)
Structure (keratin)
Writing quiz 9/20 vvv
Four Levels of Protein Structure
Primary
Amino acid (AA) sequence
20 different AA’s
peptide bonds link AA’s
R group = side chains
Properties:
hydrophobic
hydrophilic
ionic (acids & bases)
“amino” : -NH2
“acid” : -COOH
Please tell us how a protein comes together
Secondary
Gains 3-D shape (folds, coils) by H-bonding
Alpha (α) helix, Beta (β) pleated sheet
Basic Principles of Protein Folding
Hydrophobic AA buried in interior of protein (hydrophobic interactions)
Hydrophilic AA exposed on surface of protein (hydrogen bonds)
Acidic + Basic AA form salt bridges (ionic bonds).
Cysteines can form disulfide bonds.
Tertiary
Bonding between side chains (R groups) of amino acids
H bonds, ionic bonds, disulfide bridges, van der Waals interactions
Quaternary
2+ polypeptides bond together
9/20 primary structure to Quaternary structure
Chaperonins: assist in proper folding of proteins
Protein structure and function are sensitive to chemical and physical conditions
Unfolds or denatures if pH and temperature are not optimal
solidity (very salty) can denature
Can nature and denature naturally or can denature and never come back (faulty protein)
change in structure = change in function
Nucleic Acids - Function: store hereditary info
DNA | RNA |
---|---|
Double-stranded helix N-bases: A, G, C, Thymine Stores hereditary info Longer/larger Sugar: deoxyribose | Single-stranded N-bases: A, G, C, Uracil Carry info from DNA to ribosomes tRNA, rRNA, mRNA, RNAi Sugar: ribose |
Nucleotide = Sugar + Phosphate + Nitrogen Base
Carbohydrates
**__Fuel __**and building material
Include simple sugars (fructose) and polymers (starch)
Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O
monosaccharide → disaccharide → polysaccharide
Monosaccharides = monomers (eg. glucose, ribose)
Polysaccharides:
Storage (plants-starch, animals-glycogen)
Structure (plant-cellulose, arthropod-chitin)
Starch = α glucose monomers
Cellulose = β glucose monomers
Lipids
Fats (triglyceride): store energy
Glycerol + 3 Fatty Acids
saturated, unsaturated, polyunsaturated
Steroids: cholesterol and hormones
Phospholipids: lipid bilayer of cell membrane
hydrophilic head, hydrophobic tails
Saturated | Unsaturated / Polyunsaturated |
---|---|
“saturated” with H | Have some C=C, result in kinks |
In animals | In plants |
Solid at room temp. | Liquid at room temp. |
Eg. butter, lard | Eg. corn oil, olive oil |