Macromolecules

Dehydration Synthesis

when monomers combine to create polymers, releasing water molecules as a by-products — uses energy

Hydrolysis

when water molecules are added to split molecules — releases energy

Glucose Formula

C2H12O6

Glycosidic Bond

type of covalent bond formed via dehydration synthesis between monomers

Disaccharide Formula

C12H22O11

Polysaccharide

long chain of monosaccharides linked by glycosidic bonds (branched/not), can be alpha/beta forms

Glycerol Formula

C3H8O3

Omega-3 Fatty Acids

fatty acids not synthesized by the human body, polyunsaturated fats; 3rd carbon at end of hydrocarbon connected to neighboring carbon

Alpha-linoleic acid (ALA)

C18H30O2

Eicosapentaenoic acid (EPA)

C20H30O2

Docosahexaenoic acid (DHA)

C22H32O2

Phospholipids

2 fatty acids (one saturated and one unsaturated) + phosphate and glycerol head

Waxes

long-chain, hydrophobic fatty acids

Steroids

hydrophobic, water insoluble, four-linked carbon rings, -OH functional group

Triglycerides

glycerol backbone + fatty acid chains of hydrocarbons where carboxyl group is attached (also called triacylglycerol)

Amylase Formula

C6H10O5, breaks down sugars

Lipase Formula

C11H9N3O2+, breaks down fats

Pepsin Function

breaks down smaller proteins

Trypsin Function

breaks down large polymer proteins

Hemoglobin Function

transports oxygen in the blood

Albumin Function

regulates osmotic pressure and transports substances in the blood

Actin Function

structural support, movement of cell surface

Tubulin Function

forms microtubules for cell structure and transport

Keratin Function

provides structural support and protection for cells, skin, hair, and nails

Insulin Function

moves glucose from blood throughout body

Thyroxine Function

regulates development and metabolism

Denaturation

when changes in temperature, pH, and chemical composition cause changes in form, and thus function

Peptide Bond

covalent bond between two amino acids

N-terminal

end of a peptide chain with a free amino group, determined peptide sequence

Polypeptide

a chain of amino acids

Protein

a chain of amino acids that have been folded

Primary Structure

unique sequence of amino acids determined by gene encoding

Secondary Structure

folding patterns:

Alpha-helix: held by hydrogen bonds between oxygen and carbonyl of one amino acid and other four amino acids further along

Beta-pleated: pleats formed by hydrogen bonding between backbone and chain

Tertiary Structure

three dimensional structure due to chemical interactions

Quaternary Structure

interaction of several subunits for stabilization, when proteins have 2+ polypeptide chains

Chaperones

proteins that assist in folding process by preventing aggregation

Purines

type of nitrogenous base with 2-carbon nitrogen rings; adenine and cytosine

Pyrimidines

type of nitrogenous base with 1-carbon nitrogen ring; uracil, guanine, thymine

5’ - 3’ Phosphodiester Linkage

a bond formed between the 5’ phosphate group of one nucleotide and the 3’ hydroxyl group of another, involving removal of 2 phosphate groups

Antiparallel Orientation

arrangement of strands in DNA where 5’ carbon end faces 3’ carbon end of matching strand, permitting hydrogen bonding and transcription with complementary synthesis

messenger RNA

carries genetic information in sets of codons

Codon

sets of 3 bases to be read by mRNA

ribosomal RNA

ensures proper alignment of mRNA and ribosomes, catalyzing formation of peptide bonds between aligned amino acids

transfer RNA

carries correct amino acid to site of protein synthesis

microRNA

regulation of gene expression and apoptosis

transcription

DNA dictates mRNA structure

translation

RNA tells the structure being given to produce