Biological Molecules

Amino Acid

Polar oxygen, hydroxyl (OH)

Non Polar, hydrophoc, C, H

Polar charged

OH- acidic

H+ basic

Nhs, COo, h. R

dehydration polypeptides with H and O

eNgine, Caboose terminus

Protein Structure

Primary, linear order, peptide bonds release water molecuels

Secondary, alpha helix, beta pleated sheets, hydrogen bonds

Tertiary folding, SH covalent disuflate bridge

quaternary interactions

Proteins

made from amino acids (CHON, S)

central carbon, side chain, amino grop, carboxyl

carbon rich hydrophobic

hydrophilic interact with water

defense antibodies

transport pumps membrane

enzymes catalyze

communication, cell surface (insulin) signlaling pathways

storage, keep iron

structure, collagen

Nucleotides

DNA, RNA

phosphate, 5 carbon sugar, base

CG 3 bonds

AT AU 2 hydrogen bonds

sugar phosphate backbone

Polymeriuzation

phosphate and OH group on backbone to new bodn add nucleotide

5’ beginning to 3’, add on 5’ to 3’ end

antiparallel oposite

carbs

energy, strucutre, signalling

glucose

h up alpha

h done beta glucose

starch

glycogen, highly branch

cellulose, plants, linear, clsoe strong wall, not flexible

rings or linear

lipids

not polyemrs

hydrophobic, nonpolar

triglycerides, fats, three tails

• glycerol, 3 fatty acids, dehydration 3H2O ester bond

• store energy

phospolipids, surround membrane

• polar head hydrophilic, charged nitrogen, phosphate

• glycerol backbone

• carboxyl gorups

• nonpolar tail hydrophobic

steroids and waxes

• cholesterol, estrogen, testosterone, four rings

defined by chemistry not structure