IBHL Bio:Organic Chemistry

Monomers of nucleic acids

Nucleotides (be able to draw one)

Monomers of proteins

Amino acids (be able to draw one)

Structure of carbohydrates

1:2:1 ratio between carbon, hydrogen, and oxygen

Most common elements in living things

carbon (C), hydrogen (H), oxygen (O), nitrogen (N)

Elements important to living things

sulfur (S), calcium (Ca), phosphorus (P), iron (Fe), sodium (Na)

Properties of water

Polar, cohesive, has high specific heat, and is an excellent solvent.

Organic Molecules

Contain carbon and hydrogen and are found in living organisms.

monosaccharides

glucose, galactose, fructose

disaccharides

maltose, lactose, and sucrose

disaccharides

maltose, lactose, and sucrose

polysaccharides

starch, glycogen, and cellulose

Draw me!

amino acid

Draw me!

glucose

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fatty acid

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nucleotide

condensation reaction

two monomers react to form a dimer, water is a product.

hydrolysis reaction

one dimer (or polymer) becomes two monomers, water is a product.

functions of lipids

energy storage, thermal insulation, protection of internal organs, major component of cell membranes.

function of amino acids

create proteins

functions of carbohydrates

energy and structural support

functions of nucleotides

passage of genetic information from parent to offspring, creation of proteins.

function of proteins

structural support, transport, movement, defence, metabolism

globular proteins

water soluble, have round (globby) shape.
Enzymes are typically globular proteins

fibrous proteins

water insoluble, long, stringy shape.
Collagen is an example of a fibrous protein

enzymes

proteins that catalyze chemical reactions.

allosteric inhibition

enzyme inhibition caused by binding to a site other than the active site

competitive inhibition

enzyme inhibition caused by binding of an inhibitor to the active site, blocking the substrate

coenzyme

a molecule (often a vitamin) that increases enzyme activity by binding to an allosteric site.

Primary Protein Structure

Order of amino acids. Peptide bonds hold amino acids together.

Secondary Protein Structure

Repeated "motifs" or patterns in the polypeptide that form either a helix or a pleated sheet. Stabilized by hydrogen bonds.

Tertiary Protein Structure

Interactions between the variable "R" groups that cause the polypeptide's "nascent" folded form. Bonds can be ionic, covalent, hydrogen, or disulfide.

Quaternary Protein Structure

Interactions between several polypeptides to form the completed and functioning protein.