Bio Test 1

Front 1

macromolecule

Back 1

large organic polymer

Front 2

polymer vs monomer

Back 2

a polymer is a large molecule consisting of similar or identical subunits (monomers)

Front 3

polymerization rxn/ dehydration rxn

Back 3

builds polymers, requires energy and enzymes

Front 4

hydrolysis

Back 4

breaks polymers down by adding water, releases energy but also requires it

Front 5

monosaccharides

Back 5

carbs: simple sugars monomers
Fxn: components of structural carbs or provides energy and nutrition to cells
Ex: glucose, fructose, galactose

Front 6

Disaccharides

Back 6

2 monosaccharide slinked via dehydration synthesis and held by a glucosidic linkage (covalent bond)
Ex: glucose + glucose= maltose
glucose + Galactose= lactose
Glucose + fructose= sucrose

Front 7

Glucosidic linkage

Back 7

covalent bond in disaccharide

Front 8

energy storage polysaccharides

Back 8

starch (plants--> glucose stored in leukoplasts)
Glycogen (animals--> stored in muscles and liver)

Front 9

structural polysaccharides

Back 9

cellulose
- plants
- polymers of glucose= insoluble fiber
-symbiotic microbes digest cellulose
Chitin
-exoskeletons and cell walls in arthropods and fungi
-tough and leathery
-mineralizes with CaCO3
-used in sitiches

Front 10

Lipids

Back 10

non polar, hydrophobic

Front 11

4 classes of lipids

Back 11

waxes, fats/oils, phospholipids, steriods

Front 12

waxes

Back 12

used for waterproofing

Front 13

structure of fats

Back 13

1. gylcerol (3 carbon alcohol)
2. 3 fatty acids (hydrocarbon chains with carboxyl)
3. ester linkage (btwn, carboxyl of fatty acid and hydroxyl of glycerol)

Front 14

Saturated Fats

Back 14

solid at room temp., only single bonds between carbons
saturated with respect to hydrogen

made by animals

Front 15

unsaturated fats

Back 15

liquid at room temperature,at least one double bond within hydrocarbon chain (forms kinks in chain)
not saturated with respect to hydrogen

made by plants, seeds, and fish

Front 16

Trans fats

Back 16

produced by hydrogenation

Decrease HDL
- lots of protein, less cholesterol 'good'

Increase LDL
-lots of cholesterol less protein 'bad'

Front 17

Function of Lipids

Back 17

1. energy storage
2. cushioning/protection
3. insulation (subcutaneous fat protects from change in temp)

Front 18

Phospholipid structure

Back 18

glycerol, 2 fatty acids, phosphate group

Front 19

Phospholipid fxn

Back 19

'dual nature' ambivalent behavior in water
hydrophilic head
hydrrophobic tail

make up cell membranes in phospholipid bilayers

Front 20

micelles

Back 20

phospholipid rings spontaneously formed

Front 21

Steriod Structure

Back 21

4 fused carbon rings with varied attachments

Front 22

Steriod fxn

Back 22

cholesterold (component of cell membranes)
steriod hormones (testosterone and estradiol)

Front 23

Nucleic Acid Fxn

Back 23

1. regulate all cell functions
2. hereditary material
3. instructions for protein synthesis

Front 24

Nucleic Acid Structure Monomers

Back 24

monomer: nucleotides
1. phospate
2. pentose
DNA deoxyribose
RNA ribose
3. nitrogenous base

Front 25

Purines

Back 25

2 interlocked rings

Adenine and Guanine

Front 26

pyrimidines

Back 26

one single ring

cytosine
thymine, uracil (only DNA)

Front 27

Nucleic Acid Structure Polymers

Back 27

RNA single stranded
DNA double helix held together by hydrogen bonds

Front 28

phosphodiester bonds

Back 28

link sugar to phosphate in nucleic acid polymers

Front 29

Protein Fxn

Back 29

diversity functions depends on conformation

Front 30

Protein monomer

Back 30

amino acid

Front 31

Structure of an amino acid

Back 31

amino group, carboxyl group, hydrogen, side chain 'R' group

Front 32

"R" group

Back 32

warible group, 20 different amino acids with different "R" groups

Front 33

three possible inoic states of an amino acid

Back 33

1. NH3+ & COOH
2. NH3+ & COO-
3. NH2 & COO-

Front 34

polymerization

Back 34

polymer becomes a polypeptide via protein synthesis

Front 35

peptide bonds

Back 35

link amino to carboxyl between amino acids

Front 36

"native conformation"

Back 36

shape of protein under normal biological conditions, spontaneous folding

Front 37

denaturation

Back 37

loss of native conformation caused by temperature change, change in pH, organic solvents (nonpolar)

Front 38

Primary structure

Back 38

amino acid sequence determined by DNA

Front 39

Secondary Structure

Back 39

hydrogen bonds between amino and carboxyl groups on different amino acids

does not involve side chains

e. alpha helix and beta pleated sheet

Front 40

Tertiary structure

Back 40

interations between side chains
ex. hydrogen bonds and hydrophobbic interactions and inco/covalent bonds and disulfide bridges

Front 41

disulfide bridges

Back 41

interactions between sulfhydryl groups

Front 42

Quaternary Structure

Back 42

multipple polypeptide fold together

Front 43

determining factors in protein conformation

Back 43

physical and chemical env. in addition to primary structure

Front 44

metabolism

Back 44

totality of an organisms chemical rxns

Front 45

catabolic pathway

Back 45

exergonic, break things down

Front 46

exergonic

Back 46

release energy

Front 47

anabolic pathway

Back 47

endergonic, build things

Front 48

endergonic

Back 48

absorb energy

Front 49

energy coupling

Back 49

linking a catabolic/energy yielding process to an anabolic/energy absorbing process

Front 50

1st law of thermodynamics

Back 50

conservation of energy

Front 51

2nd law of thermodynamics

Back 51

entropy (disorder) inceases in nature

Front 52

ATP

Back 52

adenosine triphosphate
ATP--> ADP+ a phosphate group+energy!

3 phospates held together by high energy bonds which release energy when broken

nucleotide

Front 53

catalysts

Back 53

accelerate rxnz without being changed

enxymes are organic catalysts

Front 54

activation energy

Back 54

amount of energy reactant molecules must absorb to start rxn

Front 55

enzymes

Back 55

1. proteins
2. lower activeation energy so rxns are possible under cellular conditions
3. do not change nature of rxns, can be reused
4. very selective for which rxn they catalyze

Front 56

substrate

Back 56

substance enzyme acts upon

Front 57

active site

Back 57

region of enzyme that binds to substrate

Front 58

induced fit

Back 58

change in shape of active site in response to the substrate itself

Front 59

enzymatic cycle

Back 59

E+S--> ES--> P+E (product and unchanged enzyme)

Front 60

enzyme substrate complex

Back 60

enzyme can act on approx. 1000 substrate molecules per second

Front 61

effect of pH on enzyme activity

Back 61

change in pH causes denaturaiton

low pH causes enzyme to gain H+ and high caused enzyme to lose them therefore changing shape

Front 62

effect of temperature on enzyme activity

Back 62

increased temp yields increased substrate enzyme collions--> increased rxn rate
BUT beyond optimal temp.:
vibratory movements from increased KE disrupt bonds required for 3D structure of enxyme

Front 63

cofactors

Back 63

small non protein factors required for proper enzyme fxn

Front 64

coenzymes

Back 64

organic vitamins

Front 65

minerals

Back 65

inorganic cofactors

Front 66

competitive inhibition

Back 66

inhibitor bind to/block the active site

Front 67

noncompetitive inhibition

Back 67

inhibitor does not enter active site rather binds away from active site but changes the shape of the enzyme

Front 68

Allosteric Regulation

Back 68

binding at one site causes change elsewhere
conformational change in one subunit affects all other subunits

typically in a mulitsubunit enzyme allosteric sites exist where subunits join

Front 69

allosteric activator

Back 69

stabilizes active form of enzyme

Front 70

allosteric inhibitor

Back 70

stabilizes inactive form of enzyme

Front 71

feedback inhibition

Back 71

the product of a metabolic pathway truning off its own production by inhibiting a step in the pathway

Front 72

enzyme cooperativity

Back 72

a substrate molecule primes an enzyme to accept additional substrate molecules more readily