Semester 1 Final: The Structure & Function of Macromolecules Flashcards
dehydration synthesis
Monomers are connected by a dehydration reaction:
– One monomer provides the hydroxyl group & the
other provides a hydrogen to form a water molecule that is lost
- this process is repeated continuously with the help of enzymes
hydrolysis
Polymers are disassembled to monomers through the addition of a water molecule to breaks the bonds between monomers
– One monomer receive the hydroxyl group & the other gets the hydrogen
lipids: monomers and polymers
monomers: fatty acids and glycerol
polymers: phospholipids, fats, steroids
carbohydrates: monomers and polymers
monomers: monosaccharides
polymers: disaccharides, polysaccharides
proteins: monomers and polymers
monomers: amino acids
polymers: polypeptides
Carbohydrates: function
– in cellular respiration, stored energy is extracted from glucose molecules
– Storage material until hydrolyzed into sugar for cells
• Starch: plant storage made of glucose monomers- stored in plastids.
• Glycogen: human storage found in the liver and muscles
– Building material for protective structures
• Cellulose: part of the tough cell wall of plants
• Chitin: builds exoskeletons in arthropods & found in fungi cell walls
Lipids: function
fats provide energy storage
– Adipose in animals
– Seeds in plants
phospholipids are the main component of cell membranes (the phospholipid bilayer)
unsaturated fats and cholesterol maintain cell membrane fluidity
sex hormones (ex. testosterone and estrogen) act as chemical messengers
Proteins
– Structural support – Storage – Transport – Hormone Signaling – Defense against foreign substances – Speed up chemical reactions (enzymes) – Digestion
Protein Structure: Primary
The unique sequence of amino acids
Protein Structure: Secondary
Folds & coils in the polypeptide chain due to hydrogen bonds between repeating sections
- α helix
- β pleated sheet
- due to attraction of partially negative carboxyl group and partially positive amino group
Protein Structure: Tertiary
Overall shape of the polypeptide due to the interactions between side chains (R groups)
- Hydrophobic interactions
- Disulfide bridges
- Ionic bond
- Hydrogen bond
Protein Structure: Quaternary
-same type of interactions as tertiary structure
Two or more polypeptide chains create one protein
nonpolar and nonpolar amino acids form
hydrophobic interactions (Van der Waal)
polar and polar amino acids form
hydrogen bonds
positively charged base and negatively charged acid form
ionic bonds