AP Bio - Unit 1: Biochemisty (Macro Molecules)

What are the 4 macromolecules?

carbohydrates (sugar), lipids, nucleic acids, proteins

carbohydrate suffix

-ose

Carbohydrates function

energy and structure

Carbohydrate properties

CHO (1:2:1), polar, hydrophilic

carbohydrate structure

hexagon/pentagon with hydroxyl

mono-sacchride examples

glucose, fructose, galactose

di-sacchride examples

sucrose, maltose, lactose

polysacchride examples

starch, fiber, glycogen

Lipid function

energy, insulation and protection

lipid properties

non-polar, no monomers, CHO no ratio

3 types of lipids

triglycerides, phospholipids, steroids/cholestrol

triglyceride structure

glycerol + 3 fatty acid chains, overall nonpolar

triglyceride types

saturated and unsaturated

Phospholipid structure

Phosphate group + glycerol + 2 fatty acids (polar)

phospholipid function

cell membrane structure

cholesterol structure

Hydrocarbon tail attached to 4 carbon rings and OH group. nonpolar

cholesterol function

membrane integrity and hormones

Nucleic Acid function

store and transmit genetic information

nucleic acid properties

CHONP, polar

Nucleic acid monomer name

nucleotide

nucleotide structure

phosphate group + pentagon (sugar) + nitrogenous base

nucleic polymers

DNA and RNA

DNA Structure

double helix

RNA structure

single helix

Protien function

enzymes and cell functions

protein properties

CHONS

Protein monomer

amino acids

amino acid structure

amino group + central carbon, hydrogen and R group + carboxylic group

how many amino acids are there?

20 amino acids, 9 are essential

how are amino acids bonded

di-peptide bonds

whats the primary protein structure

chain of amino acids, the order of amino acids determines the structure of the protien

What's the secondary structure of a protein?

the chain folds on itself, held together with Hydrogen bonds, fold into either a pleated sheet or helix

What is the tertiary structure of a protein?

R-group interactions, held together with hydrogen bonds, ionic bonds, and di-sulfide bonds

What's the quaternary structure?

more R-group interactions, globlar protiens, has subgroups/subunits

whats protein denaturation

the unfolding of a protein/loss of 3rd and 4th group interactions. caused by heat or pH