Chapter 5: Structure and Function of Macromolecules Flashcards
Elements that make carbohydrates? Their ratio?
Carbon, hydrogen, and oxygen
1:2:1
What are monosaccharides? Primary function?
A monomer of carbohydrates; sugars that can’t be made into simpler sugars i.e. pentoses (ribose, deoxyribose) and hexoses (glucose, fructose, galactose). PF= to provide energy
Two groups of polymers in carbohydrates?
Disaccharides (maltose, sucrose, lactose) and polysaccharides (starch, glycogen, cellulose, chitin)
PF of starch?
Plant energy storage compound (seeds, special structures)
PF of cellulose?
Plant structural component (cell walls)
PF of glycogen?
Animal energy storage compound (liver and muscles)
What elements make up lipids? H:O ratio?
Carbon, hydrogen, and oxygen; >2:1
PF of fats?
Energy storage, insulation, physical protection
PF of oils?
Lubricate skin, prevent it from cracking, make skin hydrophobic (same w/ hair)
PF of steroids?
Hormonal communication, stabilize membrane structure (cholesterol strengthens cell membranes)
PF of phospholipids?
Cell membrane structure
Saturated vs unsaturated fatty acids?
Saturated- no double bonds between carbon atoms
Unsaturated- double bonds between carbon atoms
Distinguish between the head and the tail of a phospholipid, and explain its importance in membrane structure
The head of a phospholipid is polar while the tails are nonpolar; allows water to pass through the membrane but not stay
What elements make up proteins?
Carbon, hydrogen, oxygen, nitrogen, and sulfur (in small amounts)
What are amino acids? How many are there?
The subunit monomer building blocks of proteins composed of a carboxylic and amino group; 20 kinds
How do amino acids differ from one another?
The side groups/ R groups; either nonpolar, polar, or charged/ionic
Primary structure
A protein’s unique sequence of amino acids; determined not by the random linking of amino acids, but by inherited genetic information…
3 letters=1 codon=1 amino acid
Secondary structure
The coils and folds of a protein; the result of hydrogen bonds between the repeating constituents of the polypeptide backbone
Tertiary structure
The overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids…
Subunit
Quaternary structure
The overall protein structure that results from the aggregation of these polypeptide subunits…
Many subunits
What is a protein’s conformation and why is it important?
It’s shape; allows for it to perform a specific function
Protein functions?
Support, movement, transport, buffering, metabolic regulation, coordination and regulation, defense, storage
What’s denaturation?
Proteins unraveling and losing their shape becoming inactive
5 characteristics of an enzyme?
Organic catalysts, proteins, specific for substrate, lower activation energy, necessary for biochemical reactions to occur
