Bio Lect 1

Front 1

Major groups of lipids

Back 1

1. fatty acids
2. triacylglycerols
3. phospholipids
4. glycolipids
5. steroids
6. terpenes

Front 2

fatty acid structure

Back 2

long chain of carbons with carboxylic acid on one end

usually even number of carbons, make in humans 24

sat or unsat

Front 3

phospholipid stucture

Back 3

like tryacylglcerol but phosphate group replaces one of fatty acids on glycerol

means one end is polar, other nonpolar
amphipathicc

Front 4

steroid structure

Back 4

4 ring structures

Front 5

eicosanoids

Back 5

20 carbon fats

include: prostaglandins, thromboxanes, leukotrienes

Front 6

lipoprotein structure

Back 6

lipid core surrounded by phospholipids and apoproteins

classified by density (greater lipid to protein ratio, lower the density)

Front 7

major functions of lipids

Back 7

phospholipids = structural component of membranes

triacylglycerols = store metabolic energy, provide thermal insulation and padding

steroids = regulate metabolic activity

some as local hormones

Front 8

amino acid structure

Back 8

amine is attached to carbon in alpha position to the carbonyl

side chain also attached to alpha carbon

hydrogen bonds between carbonyl oxygen and hydrogen of amino group

Front 9

5 forces creating tertiary structure

Back 9

1. covalent disulfide bonds bw cysteine aa
2. electrostatic (ionic) forces
3. hydrogen bonds
4. van der Waals forces
5. hydrophobic side chains

proline induces turns in polypeptide that will disrupt formation of a-helix and b-sheet formation

Front 10

funtions of globular proteins

Back 10

enzymes (pepsin)
hormones (insulin)
membrane pumps and channels
membrane receptors
intracellular and intercellular transport and storage
osmotic regulators
immune response
etc

Front 11

Denaturing agents and forces disrupted

Back 11

urea

salt of pH change

mercaptoethanol

organic solvents

heat

Hint 11

hydrogen bonds

electrostatic bonds

disulfide bonds

hydrophobic forces

all forces

Front 12

cytochromes

Back 12

proteins that require a prosthetic heme group to function (conjugated protein)

Front 13

anomers of glucose

Back 13

alpha - anomeric carbon and methoxy group are on opposite sides of carbon ring

beta = they are on the same side

Front 14

glucose polymers and linkages

Back 14

starch - alpha (1-4)

glycogen- alpha (1-4) and alpha (1-6) at branches

cellulose - beta (1-4) = undigestable

Front 15

components of nucleotides

Back 15

five carbon sugar

nitrogenous base (A, T, C, G, U)

phosphate group

Front 16

phosphodiester bond

Back 16

between phosphate group and 3rd carbon of pentose

therefore written 5'-3' (because say base first)

Front 17

nucleotides

Back 17

ATP, cyclic AMP, NADH, FADH2

as well as the usual...

Front 18

Functions of minerals

Back 18

help form electrochemical gradients - therefore assist in transport

strengthen matrix (ie hydroxyapatite in bone)

cofactors (iron in heme)

Front 19

induced fit model

Back 19

shape of both the enzyme and the substrate are altered upon binding

Front 20

saturation kinetics

Back 20

as the relative concentration of substrate increases, the rate of the reaction increase, but only to maximum rate Vmax (proportional to enzyme concentration)

also affected by temperature (until denatures...) and pH

Front 21

cofactor

Back 21

required by many enzymes in oder to reach optimal activity

coenzymes or metal ions

Front 22

coenzymes

Back 22

many are vitamins or derivatives

two types - cosubstrate - transfer some chem group to another substrate (ATP is example!) another enzyme reverts to original form

prosthetic group - remain covalently bound to enzyme thru reaction, emerge unchanged

Front 23

irreversible inhibtor

Back 23

bind COVALENTLY to enzymes during function

Front 24

competative inhibitors

Back 24

bind noncovalently to active substrate

can be overcome by increasing substrate concentration

decreases Km because disruptes bond bw enzyme and substrate

Vmax still same

Front 25

noncompetitive inhibitors

Back 25

bind covalently to enzyme at spot other than active site

dont prevent substrate from binding

can commonly acto on more than one enzyme (becasue doesn't resemble substrate)

lower Vmax - bc less enzyme to act

Front 26

enzyme regulation

Back 26

1. proteolytic clevage - state as zymogen or proenzyme - irreversibly activated
2. reversible covalent modification - activated or deactivated by phosphorylation
3. control proteins - protein subunits that associate w certain enzymes to activate or inhibit activity - G-proteins
4. allosteric interactions - binding of activator or inhibitor at specific binding site on enzyme - ie feedback inhibitors

Front 27

Cooperativity

Back 27

positive and negative

first substrate binds to enzyme and changes shape allowing other substrates to bind more easily (positive)
-ie hemoglobin curve

Front 28

lyase

Back 28

aka synthase
catalyzes the addition of one substrate to a double bond of another substrate

Front 29

ligase

Back 29

aka synthetase
catalyzes addition of one substrate to double bond of another but needs energy from ATP or other nucleotide

Front 30

kinases

Back 30

enzymes that phosphorylate something

Front 31

phosphatases

Back 31

enzymes that dephosphorylates something

Front 32

glycolysis

Back 32

series of rxns that breaks glucose into 2 pyruvates

net plus 2 ATP, 2 NADH
(2 ATP added at beginning tho; 2nd P commits molec to pathway)

in cytosol of cell

pyruvate on to krebs orr ferments

Front 33

fermentation

Back 33

reduction of pyruvate to ethanol or lactic acid; oxidation of NADH back to NAD+ (restored for use in glycolysis as coenzyme)

Front 34

aerobic respiration

Back 34

if O2 present, pyruvate and NADH move into mito matrix
(may use one ATP for NADH across inner mem)
- pyruvate to acetyl CoA (plus NADH and CO2)
- Krebs cycle and then ETC

Front 35

Acetyl CoA in cellular respiration

Back 35

acts as a COENZYME transfering 2 Carbons to oxaloacetic acid (making citrate) in Krebs cycle

Front 36

Krebs cycle

Back 36

Net:
1 ATP
3 NADH
1 FADH2
TIMES 2! one per acetyl CoA
substrate phosphorylation

Front 37

Triglycerides and Krebs

Back 37

Fatty acids converted into acyl CoA - 2 Cs cleaved at a time to acetyl coA (plus FADH2 and NADH per cleavage)

glycerol in PGAL

Front 38

ETC

Back 38

inner membrane of mito
H+ pumped across to intermembrane space (lower pH)

proton-motive force=
NADH - 2 or 3 ATP
FADH2 - 2 ATP (further along)
via ATP synthase
oxidative phosphorylation
final e acceptor is oxygen

Front 39

Net ATP from aerobic resp

Back 39

36 ATP
(includes glycolysis)