Mcat Bio Chap1

Front 1

what is the difference between ehat energy and potential energy

Back 1

heat is the movement of molecules
potential is stored in chemical bonds

Front 2

what is the first law of thermodynamics

Back 2

law of conservation of energy that energy in the universe is constant

Front 3

what is the second law of thermodynamics

Back 3

entropy tends to increase

Front 4

what is the equation for gibbs free energy

Back 4

change in G = Chane in H - Tchange in S

Front 5

what is the equation for enthalpy

Back 5

H= E - PV

Front 6

given that cellular reactison take plac ein the liquid phase how is H related to E in a cell?

Back 6

H is approx equal to E since the change in volume is negligible

Front 7

what is the difference between exergonic and exothermic

Back 7

one is the energy that exits a system as in change in G

exothermic is reaction related to H in which heat is transferred out

Front 8

signs of thernodyamic quantities are assigned fromt he point of view of the system not the surroundings of the universe. t or f

Back 8

True

Front 9

The value of change in G depends on _____ and ______

Back 9

concentration of reactants
conc of products

Front 10

what is the difference between K and Keq

Back 10

Keq has to do with equilibrium. K is just based on what is there right now

Front 11

define equilibrium

Back 11

the point where the rate of reaction in one direciton equals the rate of reaciton in the other

Front 12

what two things determjine spontaneity

Back 12

intrinsic properties of the reactants and products change in Gdegree

the conc of reactants and products RTlnK

Front 13

What is the equation for standard free enrgy change

Back 13

G' = -RTlnKeq

Front 14

what does Keq =

Back 14

conc products/conc reacants AT EQUIL

Front 15

what is the full equation for Gibbs

Back 15

change in G = G' + RTlnK

Front 16

how does the change in G fro a reaction burning or oxidizing sugar in a furnace compare to the changfe in G when sugar is broken down oxidized in a human

Back 16

they are teh same. it depends on the result not the pathway

Front 17

define chemical kinetics

Back 17

the study of reaction rates

Front 18

define activation energy

Back 18

the energy required to produce the transient intermediate

Front 19

define catalyst

Back 19

lowers the energy of activation of a reaction without changing the change in G. It lowers the Ea by stabilizing the transition state making its existence less thermodynamically unfavorable

Front 20

enzymes are _____

Back 20

catalysts

Front 21

as catalysts, do enzymes have a kinetic role or a thermodynamic role?

Back 21

kinetic

Front 22

thermodynamically unfavorable reactions in the cell can be driven forward by ____ _____

Back 22

reaction coupling

Front 23

what is the favorable reaction that the cell can use to drive unfavorable reactions

Back 23

ATP hydrolysis

Front 24

do enzymes influence rate, favorability or both?

Back 24

JUST rate

Front 25

the active site has aa residues taht ____ the transition state of a reaction

Back 25

stabilize

Front 26

is it possible that aa located far apart from each other in the primary protein seq may play a role in the formation of the same active site

Back 26

yes proteins are folded

Front 27

at equil, G =

Back 27

0

Front 28

the active site for enzymes is generally highly specific in its substrate recognition. It may even be able to distinguish between sterioisomers. ``This is called...

Back 28

stereospecifity

Front 29

what aa are in animals
sugars?

Back 29

L
D

Front 30

what is a protease

Back 30

protein cleaving enzyme

Front 31

what is a recognition pocket

Back 31

enzymes have it near the active site that attracts certain residues on substrate polypeps

Front 32

what are four ways to regulate enzyme activity

Back 32

covalent modification
proteolytic cleavage
association wiht other polypep
allosteric regulation

Front 33

what is an exampel of covalent modification

Back 33

phosphorylation of an enzyme to activate it

Front 34

what is an exmpale of proteolytic cleavage

Back 34

zymogens to active enzymes

Front 35

what are zymogens

Back 35

enzymes that are created to be inactive until cleave by a protease

Front 36

removal of the regulatory subunit results in continuous rapid catalysis by the catalytic subunit this is called....

Back 36

constitutive activity

Front 37

is the allosteric regulator covalent? reversible?

Back 37

no
yes

Front 38

what is feedforward stimulation

Back 38

stimualtion of an enzyme by ti ssubstrate or by a molecule used in the synthesis of the substrate

Front 39

what does reaction rate depend on

Back 39

concentration fo the substrate and enzyme

Front 40

saturation is denoted by

Back 40

vmax

Front 41

what does tense mean

Back 41

the conformatio of enzyme with decreased affienity

Front 42

what are cooperative enzymes

Back 42

have more thna one active site where one substrate binding enhances the binding of the other

Front 43

what kind of curve shows cooperative binding

Back 43

steep sigmoidal curve

Front 44

what is the relationship between the two motion of allosteric and cooperative?

Back 44

allosteric is other site
cooperative takes place at the active state because it is the substrate that is binding

Front 45

what kind of inhibition lowers the vmax

Back 45

NONcompetitive

Front 46

photosynthesis is the process by which plants store energy in teh form of ___

Back 46

carbs in bond energy

Front 47

what are the three meanings of oxidize

Back 47

loss of electrons
loss of H
addition of O bonds

Front 48

the way we extract energy from glucose is called

Back 48

oxidative catabolism

Front 49

is O2 to H2O oxidation or reduction

Back 49

red

Front 50

what enzyme is for G to G6P

Back 50

hexokinase

Front 51

what enzymes is for F6P to F1,6BP

Back 51

phosphofructokinase

Front 52

what is the committed step

Back 52

F1,6BP
to triglyceride

Front 53

what takes PEP to pyruvate

Back 53

pyruvate kinase

Front 54

would a limiting supply of NAD+ inhibit or stimulate glycolysis

Back 54

inhibit becuase lots of substrate doesn't encourage making of more

Front 55

what happens in pyruvate dehydrogenase complex

Back 55

oxidative decarbosylation

Front 56

define prostehtic group

Back 56

a nonprotein molecule covalenty bound to an enzyme as part of the enzymes active site

Front 57

what is OAA

Back 57

oxaloacetate

Front 58

is the inner membrane of the mitochondria permeable?

Back 58

no but the outer is

Front 59

how do bacti make ATP since there is no membrane space to create a gradient

Back 59

atp synthase

Front 60

how many protons per molecule of ATP

Back 60

4

Front 61

how many ATP are made for euk? prok?

Back 61

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