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Flashcards in Chemistry Of Bio Deck (49):
0

5 properties of water

1. Excellent solvent- break up charged ionic molecules
2. High heat capacity and heat of vaporization- must add a lot of energy to warm up water
3. Ice floats- expands as it freezes because h bonds become more rigid and form crystal that keeps molecules apart
4. Cohesion/surface tension- attraction between like substances due to h bonds
5. Adhesion- attraction of unlike molecules, capillary action

1

Functional groups:
1. OH
2. COOH
3. NH2
4. PO3
5. C-double bond-O
6. CH3

1. hydroxyl
2. carboxyl
3. amino
4. phosphate
5. carbonyl (aldehyde and ketone)
6. methyl - nonpolar, hydrphobic

2

what determines whether a monosaccharide is alpha or beta

position of H and OH on ANOMERIC (1st) carbon

3

1. glucose + fructose
2. glu + galactose
3. glu + glu

1. sucrose
2. lactose
3. maltose

4

bond creation and destruction in polysac

create with dehydration, break with hydolysis

5

starch, glycogen, cellulose, chitin - compare and contrast

starch: polymer of alpha-glucose molecules, store energy in plant cells
glycogen: polymer of alpha-glucose molecules, store energy in animal cells
*they differ in their branching patterns
cellulose: polymer of beta-glucose, structural molecules for walls of plant cells/wood
chitin: similar to cellulose, but each beta-glucose has N-containing group attached to ring; fungal cell walls and insect exoskeleton

6

triglycerides (triacylglycerides) - structure

3 FA's attached to glycerol backbone
saturated = all sigmas, no pi -- straight chains stack densely and form fat plaque

7

phospholipid structure

2 FA's and phosphate group (+R) attached to glycerol backbone -- amphipathic

8

steroids structure

backbone of 4 carbon rings; hormones and cholesterol

9

5 lipid derivatives:

1. phospholipids
2. waxes
3. steroids
4. carotenoids
5. porphyrins (tetrapyyroles)

10

waxes

esters of FA's and monohydroxylic alcohols; used as protective coating or exoskeleton (lanolin)

11

carotenoids

FA carbon chain with conjugated double bonds and 6 membered c-rings at each end; pigments - carotenes, xanthophylls

12

porphyrins (tetrapyyroles)

4 joined pyrrole rings (pyrrole = 5 C aromatic ring, 2 pi bonds, NH at bottom); complex with metal **prophyrin heme complexes with Fe in hemoglobin; chlorophyll w/Mg

13

glycolipids

like phospholipids, but carb group instead of phosphate

14

lipoproteins

lipid core surrounded by phospholipids and apolipoproteins (the proteins that bind lipids); used to transport lipids in blood because insoluble

15

membrane dynamics

cold: increase unsaturation because you want to increase fluidity with the kinks and get the lower melting point (if saturated, higher melting point so that means they will be solidified)

16

FA characteristics

unsaturated: higher boiling point but lower melting point due to increased kinks from pi bonds; pi bond increases polarity which increases bp; pi bonds decrease packing which lowers melting point

17

casein

milk protein

18

zein

protein in corn

19

ovalbumin

egg white protein

20

cytochrome

electron transport protein

21

cofactor

nonprotein molecule that assists enzyme

22

holoenzyme

union of enzyme and cofactor

23

apoenzyme/apoprotein

Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An apoenzyme together with its cofactor(s) is called a holoenzyme (this is the active form). Most cofactors are not covalently attached to an enzyme, but are very tightly bound

24

prosthetic group

when enzyme-cofactor bond is strong covalent

25

organic vs inorganic cofactors

org = vitamin (coenzyme) vs inorg = mineral (Fe2+, Mg2+)

26

simple protein

entirely aa's

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albumins and globulins

carriers and enzymes

28

scleroproteins

fibrous, structural (collagen)

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conjugated protein

simple protein + nonprotein

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lipoprotein

protein bound to lipid

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mucoprotein

protein bound to carb

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chromoprotein

protein bound to pigment molecule

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metalloprotein

protein complexed around metal ion

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nucleoprotein

protein that contains histone or protamine, bound to nucleic acid

35

secondary protein structure

3D shape due to H-bonds between amino and carboxyl groups of adjacent aa's (alpha-helix, beta pleated sheet)

36

tertiary protein structure

3D structure due to noncovalent interactions between R-groups; H-bonds, ionic bonds, hydrophobic effect, disulfide bonds, VDW are all factors

37

2 main categories of larger proteins

1. globular: somewhat soluble, dominated by 2ndary structure; enzymes, hormones, membrane pumps/channels/receptors, strorage, transport, osmotic regulation, etc
2. fibrous/structural: not soluble, dominated by tertiary structure; long polymers - maintain and add strength to cellular and matrix structure

38

purine, pyrimidine

adenine and guanine (double ring), cytosine and thymine

39

cell doctrine, 4 parts

1. all living org's = 1+ cells
2. cell is basic unit of structure, function adn organization
3. all cells come from preexisting, living cells
4. cells carry hereditary info

40

rna world hypothesis

self replicating RNA = precursor to current life; rna stores genetic info like DNA and can catalyze reactions like enzymes, but more unstable than DNA so more likely to participate in chemical reactions because of the extra OH group

41

light microscopy

basic, phase-contrast doesnt kill or stain tissue

42

electron microscopy

high res/mag, kills tissues
SEM and TEM

43

allosteric enzyme

active site (substrate binds here) and allosteric site (for allosteric effector - either activator or inhibitor binds here)

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competitive inhibition

substance that mimics substrate inhibits enzyme by binding active site; increase concentration of substrate to overcome; Vmax unchanged, Km changed

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km

Km is the substrate concentration that is required for the reaction to occur at 1/2 Vmax. In other words, it is how much substrate is needed for the reaction to occur at 1/2 its max possible rate

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Vmax

highest rate that reaction can reach

47

cooperativity

enzyme becomes mroe recpetive to additional substrate molecules after one suvtrate molecule attaches to an active site (ex: enzyme with multiple subunits, each with an active site -- quaternary structure, hemoglobin)

48

noncompetitive inhibition

subtance inhibits enzyme by binding somewhere other than active site, substrate still binds enzyme. Km unchanged, Vmax changed