Macromolecules of Life

Organic Molecules

Based on carbon

Inorganic molecules

Do not have carbon

Structural Isomers

2 or more molecules with same chemical formula but atoms are arranged differently

What breaks covalent bonds?

Hydrolysis

Polymer

Molecule consisting of many identical or similar subunit molecules linked in a chain by covalent bonds

Monomer

Each Subunit of a polymer

Macromolecule

Big polymer

Polymerization

Assembly of polymer from monomers

Common Monosaccharides

Glucose, fructose, galactose

Disaccharides

2 monosaccharides

Polysaccharides

10+ monosaccharides

Common Polysaccharides

Glycogen, amylose, cellulose, chitin

Glycogen

Storage for energy in animals

Amylose (starch)

Storage for energy in plants

Cellulose

Tightly packed, uniform, structure in plant cell walls

Chitin

Tightly packed, uniform, has a nitrogen group, structure for fungi cells and arthropods

Triglyceride Structure

Glycerol backbone, 3 fatty acid chains, Carboxyl end with hydrocarbon tail, ester linkage

Ester linkage

Covalent bond between carboxyl group and hydroxyl group

Saturated

No double bonds, rigid, straight tails, more solid, fatty

Unsaturated

1 or more double bonds, chain has a “kink” so more fluid, oily

Monounsaturated

1 double bond

Polyunsaturated

multiple double bonds

Phospholipids

Lipids of cell membranes

Amphipathic

Hydrophilic head, hydrophobic tail

Protocells

Phospholipid bilayer with organic molecules inside

Steroid

Important for signaling, cell membrane, structure

Steroid Structure

4 carbon rings with functional groups

Sterols

Steroids with single polar -OH group (cholesterol)

Steroid Hormones

Diverse structures, many different functional groups (testosterone)

Glycolipid

Lipid + Carbohydrate

Lipoprotein

Lipid + protein

Protein Primary Structure

Linear sequence of amino acids joined by peptide bonds in a polypeptide chain

Protein Secondary Structure

Coiled or folded regions in a polypeptide chain resulting from hydrogen bonding within particular sequences of amino acids

Protein Tertiary Structure

Overall three dimensional folding of a polypeptide chain, undergo conformational changes

Protein Quaternary Structure

The arrangement of polypeptide chains in a protein that contains more than one chain

Alpha Helix

Regular right hand spiral, hydrogen bonds

Beta Plated Sheets

Folded zig-zags on a plane or twisted “propeller” structure, hydrogen bonds

Random Coil

Act as hinges

Disulfide Linkages

Can hold together various parts of a protein

Domains

Large, structural subdivisions

Intrinsically Disordered Proteins (IDPs)

Flexible conformations (signaling molecules)

Transcription

DNA → RNA

Polymer

Polynucleotide Chain

Stereoisomers

Are mirror images of each other