Mcat Biology Lecture 1

Front 1

____ -The process of ATP production in the krebs cycle.

Back 1

substrate level phosphorylation

Front 2

Aerobic resp. products

Back 2

approx 32 net ATP's
1 NADH bring back 2.5 ATP (x10)
1 FADH2 bring back apprx 1.5 ATP (x2)
including 2 from glycolysis

Front 3

____
Solvent in which the chemical reactions of living cells take place.
70-80% of a cell's mass is due to this.
small polar molecule

Back 3

Water

Front 4

Unsaturated fatty acids

Back 4

contain one or more carbon-carbon double bonds.

Front 5

____ (3 names)
has a 3 carbon backbone called a glycerol, which is attached to 3 fatty acids
function is to store energy & may provide thermal insulation and may provide padding

Back 5

Triglycerides
or fats & oils
or triacyglycerols

Front 6

___ or ___
specialized cells whose cytoplasm contains almost nothing but triglcyerides.

Back 6

adipocytes
fat cells

Front 7

Hydrophilic

Back 7

water loving
polar
like dissolves like

Front 8

water molecules surround ____ a hydrophilic molecule and separate it from the group

Back 8

solvate

Front 9

most macromolecules of living cells are broken apart via ____

Back 9

hydrolysis

Front 10

____ - how most macromolecules are formed

Back 10

dehydration synthesis

Front 11

____ - any biological molecule that has low solubility in water & high solubility in nonpolar organic solvents

Back 11

lipid

Front 12

____ - a lipid. building blocks for most, but not all complex lipids. Long chain of carbons truncated @ one end by a carboxylic acid. Usually an even # of carbons w/ the max in humans being 24.

Back 12

fatty acids

Front 13

amphipathic

Back 13

one end is polar
one end is nonpolar
ex. phospholipid

Front 14

glycerol

Back 14

3 carbon backbone

Front 15

____ - glycerol backbone, w/ 2 fatty acids & a polar phosphate group w/ lies on opposite end of the nonpolar fatty acids

Back 15

phospholipid

Front 16

____- four ringed structure, includes some hormones, vitamin D & cholesterol

Back 16

steroids

Front 17

____- a 6th class of lipids which include vitamin A.

Back 17

Terpenes

Front 18

____ - contains a lipid core surrounded by phospholipids & apoproteins
can dissolves lipids in its hydrophobic core & move freely in aqueous solution due to its hydrophilic shell.

Back 18

lipoproteins

Front 19

VLDL -
LDL-
HDL-

Back 19

very low density lipoprotein
low density lipoprotein
high density lipoprotein

Front 20

Lipid functions
Phospholipids -
triacyglycerols -
fatt acids (eicosanoids) -
steroids -

Back 20

structural component of membranes
store metabolic energy, provide thermal insulation & padding
serve as local hormones
regulate metabolic activities

Front 21

____ - are built from a chain of amino acids linked together by peptide bonds.

Back 21

proteins (polypeptides)

Front 22

They are called ___ because the amine is attached to the carbon in the alpha position of the carbonyl.
approx ___ of them.

Back 22

alpha-amino acids
20

Front 23

essential amino acids

Back 23

(10) amino acids that the body cannot manufacture, must be ingested

Front 24

side chains (r group)

Back 24

how amino acids typically differ from each other
this side chain is also attached to the alpha carbon

Front 25

____ - each amino acid in a polypeptide chain

Back 25

residue

Front 26

___ - what the single chain can form
___ - are secondary structure

Back 26

alpha-helix
beta-pleated sheet

Front 27

____ - 3-d shape formed when the peptide chain curls and folds.

Back 27

tertiary structure

Front 28

(5) forces creating the tertiary structure

Back 28

1. covalent disulfide bonds between (2) cysteine amino acids on different parts of the chain
2. electrostatic (ionic) interactions mostly between acidic & basic side chains.
3. hydrogen bonds
4. van der waals forces
5. hydrophobic side chains pushed away from water (toward center of protein)

Front 29

quaternary structure -

Back 29

when 2 or more polypeptide chains bind together.
same 5 forces at work in the tertiary structure can also act to form the quaternary structure

Front 30

denatured (proteins)

Back 30

lost most of its secondary, tertiary & quaternary structure

often once the denaturing agent is removed the protein will spontaneously refold to its original conformation

Front 31

on mcat when you see nitrogen

Back 31

think protein

Front 32

Denaturing agents and forces disrupted-

Back 32

urea - hydrogen bonds
salt or change in PH - electrostatic bonds
mercaptoethanol - disulfide bonds
organic solvents - hydrophobic forces
heat - all forces

Front 33

made from carbon & water, empirical formula C(H20)

Back 33

carbohydrates
or sugars
or saccharides

Front 34

____, 6 carbon carbohydrate
c6h12o6, very common accounts for 80% of the carbohydrates absorbed by humans

Back 34

glucose

Front 35

____ - polysaccharide, branches glucose polymer w/ alpha linkages most is found in the liver and muscle cells

Back 35

glycogen

Front 36

plants form ___ from glucose
cellulose has ___ linkages

cows and termites etc have bacteria in their digestive systems that release an enzyme to digest the ____ linkages.

Back 36

starch
beta
beta

Front 37

___ - increases the rate of diffusion for glucose & other monosaccharides

Back 37

insulin

Front 38

nucleotides -

Back 38

composed of (3) components:
1. a 5 carbon sugar
2. a nitrogenous base
3. a phosphate group

Front 39

most common nitrogenous bases

Back 39

thymine (uracil)
adenine
guanine
cytosine

Front 40

nucleic acids

Back 40

DNA & RNA
formed from the nucleotides

Front 41

In typical DNA, two strands are joined by hydrogen bonds to make the structure called a ___.

Back 41

double helix

Front 42

____ - only 1 strand & no helix is formed & uracil replaced thymine.

Back 42

RNA

Front 43

Other important nucleotides

Back 43

ATP - source of readily available energy for the cell
cyclic amp - important component in many 2nd messenger systems
NADH & FADH2 - the coenzymes involved in the krebs cycle

Front 44

___ the first substrate changes the shape of the enzyme allowing other substrates to bind more easily.

Back 44

Positive cooperativity,
negative cooperativity is the opposite

Front 45

___ - if one of the products downstream in a reaction series comes back & inhibits the enzymatic activity in an earilier reaction.

"if it works it shuts off, like a thermostat"

Back 45

negative feedback
or feedback inhibition

Front 46

____ - this chemical is an enzyme and therefore probably a protein and therefore contains nitrogen and is subject to denaturation

Back 46

-ase

Front 47

inactive form of an enzyme, depending, they can reversibly or irreversibly activated

Back 47

zymogen or proenzyme

Front 48

___ - bind noncovalently to an enzyme at a spot other than the active site & change the conformation (shape) of the enzyme.
so the substrate does not even "fit" in the active site anymore

Back 48

non competitive inhibitors

Front 49

____ - compete w/ the substrate by binding reversibly w/ noncovalent bonds to the active site. (usually only for a fraction of a second)

Back 49

competitive inhibitors

Front 50

____ - agents which bind covalently to enzymes & disrupt their function. (usually highly toxic, penicillin is an example)

Back 50

irreversible inhibitors

Front 51

rxn rate ___ with ph, temp and substrate conc

Back 51

moderates, bell curve shape
moderates, bell curve shape but with a slight nudge towards higher temps
logarithmic, point at which higher conc = no gains

Front 52

___ (substrate has to wait in line on enzymes) As the relative concentration of substrate increases the rate of the reaction also increases but less & less until a max rate (Vmax) is achieved.

Back 52

saturation kinetics

Front 53

____ - shape of both the enzyme & substrate are altered upon binding.

Back 53

induced fit

Front 54

____ - example of enzyme specificity. Active site of the enzyme has a specific shape that only fits a specific substrate.

Back 54

lock & key theory
enzyme = lock
substrate = key

Front 55

___ - normally, enzymes are designed to work only on a specific substrate or group of closely related substrates.

Back 55

enzyme specificity

Front 56

The enzyme bound to the substrate is called ____.

Back 56

enzyme - substrate complex

Front 57

____ The position on the enzyme to where the substrate binds, usually with numerous non-covalent bonds.

Back 57

active site

Front 58

____ - the reactant or reactions upon which the enzyme works. Generally ____ than the enzyme.

Back 58

substrates
smaller

Front 59

____ - not consumes or permanently alterd by the reaction, only a small amount is required. do not alter the ____ of a reaction.

Back 59

catalyst (enzyme)
equilibrium

Front 60

____ - typ a globular protein occasionally a nucleic acid, act as a catalyst by lowering the activation energy and increasing the reaction rate (by magnitudes as much as thousands of trillions)

Back 60

enzymes

Front 61

____ - fluid portion of living cells

Back 61

cytosol

Front 62

combustion reaction

Back 62

(not balanced)
glucose +o2 -> CO2 + H2O

Front 63

The proton-motive force propels thru ___ to manufacture ATP.

Back 63

atp synthase

Front 64

Aerobic respiration ___.

Back 64

requires oxygen

Front 65

Glycolysis-

Back 65

1st stage of anaerobic & aerobic respiration, breaks down glucose into 2 3-carbon molecules of pyruvate (conj. base of pyruvic acid)

Front 66

___ - organic molecule, many are vitamins or their derivatives.

Back 66

coenzymes

Front 67

___ - a non-protein component that many enzymes require. can be coenzymes or metal ions (mineral)

Back 67

cofactor

Front 68

____ - feedback inhibitors bind to the enzyme & cause a conformational change. both ___ inhibitor and ___ activator

Back 68

allosteric regulation

Front 69

____ is the modification of the enzyme configuration resulting from the binding of an activetor or inhibitor at a specific binding site on the enzyme

Back 69

allosteric interaction

Front 70

in nucleic acids, nucleotides are joined together by ____ between the phosphate groups of 1 nucleotide and the 3rd carbon of the pentose of the other nucleotide forming long strands.

Back 70

phosphodiester bonds

Front 71

____ - dissolved inorganic ions inside & outside the cell
-create electrochemical gradients.
-combind & solidfy to give strength to a matrix such as hydroxyapatite in bone
-cofactors, assisting enzyme or protein function

Back 71

minerals

Front 72

___ - the # & sequence of amino acids in a polypeptide.

Back 72

primary structure

Front 73

___ - a series of protein including cytochromes w/ heme in the inner membrane of the mitochondrion.

Back 73

electron transport chain (ETC)

Front 74

____ - production of atp by the proton-motive force thru atp synthase

Back 74

oxidative phosphorylation

Front 75

intermembrane space has ____

Back 75

lower ph than the matrix

Front 76

krebs cycle or citric acid cycle -

Back 76

each turn of the krebs cycle produces 1 atp, 3 nadh, and 1 fadh2
During the cycle 2 carbons are lost as co2 and oxaloacetic acid is reproduced to begin the cycle over again.

Front 77

___ - a coenzyme which transfers 2 carbons (from pyruvate) to the 4-carbon oxaloacetic acid to begin the krebs cycle/also called the citric acid cycle.

Back 77

acetlycoa

Front 78

In the matrix, pyruvate is converted to this ___ in a reaction that produces NADH and CO2.

Back 78

Acetylcoa

Front 79

___ - the products of glycolysis move here past both membranes.

Back 79

matrix of mitochondrion

Front 80

inner mitochondrial membrane -

Back 80

less permeable than the outer.
have to pass thru to get to the mitochondrial matrix.

Front 81

____ - anaerobic respiration, includes the process of glycolysis the reduction of pyruvate to ethanol or lactic acid, the oxidation of the nadh back to the nad+

"recycles NADH back to NAD+"

Back 81

Fermentation

Front 82

Krebs cycle products -

Back 82

1 glucose = 2 turns
each turn = 1 ATP, 3 NADH, 1 FADH2

Front 83

Respiration -

Back 83

steps 2 & 3 of metabolism
w/ oxygen = aerobic
w/o oxygen = anaerobic

Front 84

metabolism -

Back 84

all cellular chemical reactions
consists of - anabolism, molecular synthesis, and catabolism

Front 85

____ - intermolecular bond
allows water to be a liquid at typical cell temps
strong cohesive forces between water molecules

Back 85

hydrogen bond

Front 86

Hydrophobic

Back 86

Water fearing
nonpolar

Front 87

Glycolysis

Back 87

2 stages, 6-carbon and a 3-carbon stage
6- expends 2 atps to phosphorylate the molecule
3- synthesizes 2 atp w/ each 3 carbon molecule (net of 2 positive)
2 pyruvate & 2 nadh molecules left & 2 net atp (4 actual)