BIO 120 - Carbohydrates & Proteins

4 classes of large macromolecules: Carbs, proteins, nucleic acids. Lipids are NOT macros.

Macromolecules are made up of monomers, Polymers of Monomers

Monomers are small molecules of identical atom structures with 2 or more binding sites

Polymers are covalently bonded monomers into a train-like link

Class of macros. is determined by type of monomers present.

Dehydration: the act of removing H2O from a monomers to create a bond of polymers (synthesis polymers)

Hydrolysis: the act of intercepting H2O in a polymer to break it apart (break down polymers)

Carbohydrates

Monomer: monosaccharides

Bond: Glycosidic

POLAR due to -OH function groups

Composed of C,H & O CH2O
Act as fuel & building materials for cells

Monosaccharides: Simplest unit of sugar

EX: Glucose, galactose, fructose

Disaccharides: Two monosaccharides joined by dehydration synthesis

Ex: Sucrose

Polysaccharides: Polymer of many monosaccharides (monomer) joined by many dehydration reactions

Ex: Starch, Cellulose

Proteins

Mono: amino acids

Bond: peptide

NONPOLAR

Proteins are involved in almost everything a protein does
THE most important building block of life

Enzymes: speed up chemical reactions, without, death
Storage: egg whites hold amino acids necessary for embryo
Transport: hemoglobin/membrane proteins
Cellular Communications: insulin to blood sugar
Movement: Muscles, actin and myosin
Immune system: antibodies vs. viruses
Response from cell to chem stimuli
Structure: hair

Amino acid - amino group bonded to carboxyl group

R group make one amino group different from another
20 diff amino acids
R groups can be polar, nonpolar, acidic, or basic

Peptides: a single chain of two or more amino acids linked by peptide bonds

Polypeptides: a chain of many amino acids (less than 50)

Forming Polypeptides: Dehydration link the carboxyl group on one amino acid yo the other amino acid via peptide (covalent) bonds

Proteins are made up of long chains of amino acids !!!

Functional protein is madeup of one or more polypeptides that have been twisted, folded, and coiled into a molecule with a unique shape
Function depends on its ability to recognize and bind to some other molecule
LARGE

Primary: refers to the amino acid single chain polypeptide that acts as a base for the other structures

Ex: DNA, the blueprint of a cell

Secondary: Alpha helix or Beta plated single polypeptides, these have different shapes due to differing primary structure, odd shape is from Hydrogen bonds, not peptide bonds

Polar R groups - H bonds

Charged R groups - Ionic bonds

Non-Polar R groups - hydrophobic

R groups - Disulfide bridge

Tertiary: also a polypeptide chain, but folds the secondary structure in globule-like molecules due to its different bond abilities like hydrophobic reactions, still held by Hydrogen bonds

Proteins vs Polypeptides: proteins are twisted into a unique shape, polypeptides are not (by themselves)

Quaternary: proteins with multiple polypeptide chains (hemoglobin)