Hydrocarbons
Functional Groups
Carbohydrates
Lipids
Proteins
100
What are the three types of hydrocarbons?
Alkanes, Alkenes, & Alkynes
100
What are the 4 functional groups?
Hydroxls, Carbonyl, Carboxyls, & Amino groups.
100
What are the elements and their ratio for a carb?
Carbs are made from C, H, and O in an 1:2:1 ratio.
100
What are 3 examples of lipids?
Oils, waxes, fats, cholesterol, and phospholipids.
100
What are all proteins (polymers) made up with (monomer) and how are ___ arranged?
All proteins are made up of 20 amino acids, all arranged differently (called isomers)
200
Which type(s) are fully saturated and why?
Alkanes; because they have the maximum amount of hydrogens bonded.
200
What do hydroxyls (OH or HO) make up?
Sugars and alcohols.
200
What are the 3 types of saccharides and how do they differ?
Monosaccharides: Simple sugars/simple carb with 1 sugar monomer (ex. glucose <-(isomers)-> fructose, and galactose)
Disaccharides: 2 sugar units/simple carb (ex. sucrose=table sugar and fructose) made by dehydration synthesis (glycosidic bond)
Polysaccharides: Many sugar units, these are complex carbs (ex. starch in plants, glycogen in animals, and cellulose)
*cellulose is for plants and animals cannot extract fiber USUALLY, but certain gut bacteria can extract it*
200
What fats (lipids) are normally solid at room temperature, and which are liquid at room temperature?
Saturated fats are normally solid at room temperature, and unsaturated fats are normally liquid.
200
What are the main jobs of proteins?
Proteins are used to build cells, act as hormones & enzymes, and do much of the work in a cell.
300
What are the formulas for alkanes, alkenes, & alkynes?
CnH2n+2
CnH2n
CnH2n-2
300
What are the differences between carbonyls and carboxyls?
Carbonyls (CO) make up aldehydes, ketones and some sugars. Carboxyls (COOH) make up amino acids, proteins, some vitamins, and fatty acids.
300
What is dehydration synthesis vs hydrolysis and what do each accomplish on a molecular level?
Dehydration synthesis is whenever 2 or more molecules bond by taking a H and an OH, then linking with the other molecule with this leftover space.
Hydrolysis breaks up a bond by forcing an H2O molecule in between a place that's bonded, causing the molecules to break up.
300
What is a triglyceride?
It's a monomer of lipids, composed of glycerol and 3 fatty acid chains.
300
How do amino acids bond, and what are the bonds called?
Amino acids bond with dehydration synthesis and they are called peptide bonds.
400
What are the differences between alkanes, alkenes, & alkynes?
Alkanes are fully saturated with only single bonds, while alkenes have at least one double bond and are unsaturated. Alkynes however have at least one triple bond and are also unsaturated.
400
Name this functional group.
Caroboxylic acid
400
What are complex carbohydrates?
Complex carbs are many sugar molecules bonded together. (ex. glycogen and starch)
400
What is the base steroid for your body to produce others?
Cholesterol.
400
What are the types of proteins ( primary, secondary, tertiary, and quaternary) and how are they built?
Primary- ribbon-like and has a specific sequece (called a polypeptide)
Secondary- Occur when protein structures coil and fold (alpha heliz-coil & beta sheet-fold). They are held together by hydrogen bonds.
Tertiary- When polypeptides join together, the tertiary structure forms an R group.
Quaternary-In a watery environment of a cell, and they become globular. It's made of 2 or more peptide chains joined together.
500
What bond would C30H58 be?
Alkyne bond
500
What is the difference between a ketone and an alehyde?
While they both contain a double carbon-oxygen bond, aldehydes have their carbonyl group on the end, and ketones have theirs in the middle of the chain.
500
What is the main purpose for carbs?
Carbs store energy.
500
Draw and label a phospholipid.
Top: Polar head (circle)-contains phosphate/hydrophilic
Two lines: Nonpolar tail and fatty acid chain/hydrophobic
500
What are enzymes and what do they do?
Enzymes (globular proteins) control the rate of chemical reactions by weakening bonds, thus lowering the amount of activation energy needed for the reaction. They act as biological catalysts.
*Each enzyme has a specific isomer for its active sight, which makes it specific for one kind of substrate*