Bio Unit 1: Chemistry of Life

weak bonds

van der Waals, H-bonds, ionic

strong bonds

covalent

polar bond - sharing of electrons

unequal

nonpolar bond - sharing of electrons

equal

properties of water

polarity, high specific heat, high heat of vaporization

cohesion

the ability of water molecules to stick together due to hydrogen bonding — allows for surface tension

adhesion

the ability of water to hydrogen bond to polar or charged objects — allow for capillary action

what elements do carbs have?

C, H, O

what elements do lipids have?

C, H, O, (P for phospholipids)

what elements do nucleaic acids have?

C, H, O, N, P

what elements do proteins have?

C, H, O, N, (S sometimes)

hydrolysis

cleaving of covalent bonds by adding water (one H added to one monomer, one OH added to the other)

dehydration synthesis

small molecules are covalently bonded together and water is lost (Loss of H and OH from monomers)

polymerization

connection of many monomers

carb structure

repeating chain of monomers

carb function

NRG, structure, stroring/transporting NRG, fiber (digestion/excretion)

carb monomer

monosaccharides

carb bonds

covalent bonds

cellulose function

structure (plant cell walls and human dietary fiber)

chitin function

structure (insects and fungi cell walls)

starch function

energy

glycogen

energy (sugar storage)lip

lipid structure

hydrophilliic head and hydrophobic tails

lipid function

long term NRG storage and cell membrane structural foundation

lipid monomer

glycerol and fatty acid

lipid bonds

covalent

saturated lipids

single bonds only

unsaturated lipids

at least one double bond, which causes the carbon chain to kink (increase double bonds, decrease saturation, and increase fluidity)fat

fats function

NRG storage, insulation

steroids function

hormones that support physiological function (growth, development, eergy for metabolism, and homeostasis).

cholesterol (steroid) function

structural stability in animal cell membrane

phospholipid function

group together to form lipid bilayers in plasma cell membrane

nucleaic acid structure

nuclotide chain (5-C sugar, phosphate, and nitrogenous base)

nucleaic acid function

DNA: directions for protein synthesis

RNA: “middle man” between DNA and ribosomes to create proteins

nucleaic acid monomers

nucleotides

nucleaic acid bonds

DNA: covalent (in between sugar and phosphate) and H-bond (in between N-bases)

RNA: covalent (in between sugar and phosphate)

what side of nucleaic acid chain is another nucleotide added to?

3’

purines

2 C-N rings - adenine and guanine

pyrimidines

1 C-N ring - cytosine and guanined

differences between DNA and RNA

DNA: sugar = deoxyribose, thymine, and double stranded

RNA: sugar = ribose, uracil, and single stranded

protein structure

amino acid chains - central C atom, carboxyl group, amine group, and R-groupprot

protein function

strucutre, nutrition, enzymes, transport, cellular defense (most diverse because of R-group)

3 possible chemical properties of proteins

(1) hydrophobic/nonpolar (2) hydrophillic/polar (3) ionic

protein monomer

amino acid

protein bonds

H-bond, hydrophobic interactions, ionic interactions, disulfide bridges, and covalent

primary structure of protein

sequence of amino acids se

secondary structure of proteins

folding, which forms interactions between adjacent amino acids to form the backbone of amino acid chain — H-bonds form alpha helices and beta pleated sheets

tertiary structure of proteins

3-D structure from formation of H-bonds, hydrophobic interactions, ionic interactions, or disulfide bridges

Fully functional!!

Interaction depends on R-groups

Goal: increase stability at lower energy state

quaternary structure of proteins

interactions between multiple polypeptides by covalent bonds (and other interactions in tertiary structure)