Biochemistry Exam 2

Front 1

Energy (E)

Back 1

the capacity to do work

Front 2

Thermodynamics

Back 2

the study of the energy transformations of physical and chemical changes of matter

Front 3

Bioenergetics

Back 3

studies the thermodynamics of living organisms.
The direction and extent of biochemical reactions

Front 4

Enthalpy (H)

Back 4

a measure of heat content

Front 5

Entropy (S)

Back 5

is a measure of disorder or randomness

Front 6

Free Energy (G)

Back 6

portion of energy that is available to do work and is related mathematically to enthalpy and entropy

Front 7

Oxidation of metabolic fuels, carbohydrates and lipids produces...

Back 7

CO2 and water

Front 8

Most metabolic energy is provided by...

Back 8

redox reactions in mitochondrion.
Mitochondrion is the power house of the cell and the major source of ATP

Front 9

Forms of energy used in the body:

Back 9

Mechanical
Thermal
Light
Chemical

Front 10

1kcal is the energy required to

Back 10

increase the temperature (completely burn or oxidize) of 1kg of water by 1C = 4.2 kj.

Front 11

What is the difference between an open and closed system?

Back 11

Open system: energy and matter can be exchanged with the surroundings.
Closed system: only energy can be exchanged

Front 12

Living organisms are open or closed systems?

Back 12

Open

Front 13

First law of thermodynamics

Back 13

energy can be neither created or destroyed but it can be transformed from one form to another

Front 14

Second law of thermodynamics

Back 14

spontaneous reactions occur in the direction that increases the total disorder of the system and its surroundings

Front 15

ΔH<0

Back 15

heat is given off during the reaction and the reaction is exothermic

Front 16

ΔH>0

Back 16

heat is absorbed during the reaction and the reaction is endothermic

Front 17

ΔH = 0

Back 17

reaction is isothermic

Front 18

ΔHo is the standard Enthalpy change, defined at...

Back 18

25C, 1 atm pressure, and 1M solute concentration

Front 19

ΔS > 0

Back 19

indicates a spontaneous reactions

Front 20

ΔG<0

Back 20

The reaction is spontaneous

Front 21

ΔG>0

Back 21

The reaction needs energy to proceed

Front 22

ΔGo is the standard free energy, defined at...

Back 22

at 25C, 1 atm pressure, and 1M solute concentration

Front 23

ΔH<0

Back 23

heat is given off during the reaction and the reaction is exothermic

Front 24

in a spontaneous reaction, ΔS ? 0 and ΔG ? 0

Back 24

ΔS > 0 and ΔG < 0 (Negative)

Front 25

ΔH>0

Back 25

heat is absorbed during the reaction and the reaction is endothermic

Front 26

When the concentration of B > A, reaction A --> B is...

Back 26

Favorable

Front 27

ΔH = 0

Back 27

reaction is isothermic

Front 28

ΔHo is the standard Enthalpy change, defined at...

Back 28

25C, 1 atm pressure, and 1M solute concentration

Front 29

ΔS > 0

Back 29

indicates a spontaneous reactions

Front 30

ΔG<0

Back 30

The reaction is spontaneous

Front 31

ΔG>0

Back 31

The reaction needs energy to proceed

Front 32

ΔGo is the standard free energy, defined at...

Back 32

at 25C, 1 atm pressure, and 1M solute concentration

Front 33

in a spontaneous reaction, ΔS ? 0 and ΔG ? 0

Back 33

ΔS > 0 and ΔG < 0 (Negative)

Front 34

When the concentration of B > A, reaction A --> B is...

Back 34

Favorable

Front 35

When the concentration of A > B, reaction A -->B is...

Back 35

unfavorable

Front 36

Protein

Back 36

Amino acid polymer with >50 amino acids
MW >10,000 daltons
May be composed of 20 different amino acids
May be comprised of one or more polypeptide chains

Front 37

Peptide

Back 37

Low molecular weight amino acid polymer with <50 amino acids

Front 38

Oligopeptide

Back 38

2-10 amino acids

Front 39

Polypeptide

Back 39

>10 amino acids

Front 40

Alanine

Back 40

Ala

Hint 40

A

Front 41

Arginine

Back 41

Arg

Hint 41

R

Front 42

Asparagine

Back 42

Asn

Hint 42

N

Front 43

Aspartic Acid

Back 43

Asp

Hint 43

D

Front 44

Cysteine

Back 44

Cys

Hint 44

C

Front 45

Glutamic Acid

Back 45

Glu

Hint 45

E

Front 46

Glutamine

Back 46

Gln

Hint 46

Q

Front 47

Glycine

Back 47

Gly

Hint 47

G

Front 48

Histidine

Back 48

His

Hint 48

H

Front 49

Iosleucine

Back 49

Ile

Hint 49

I

Front 50

Leucine

Back 50

Leu

Hint 50

L

Front 51

Lysine

Back 51

Lys

Hint 51

K

Front 52

Methionine

Back 52

Met

Hint 52

M

Front 53

Phenylalanine

Back 53

Phe

Hint 53

F

Front 54

Proline

Back 54

Pro

Hint 54

P

Front 55

Serine

Back 55

Ser

Hint 55

S

Front 56

Threonine

Back 56

Thr

Hint 56

T

Front 57

Tryptophan

Back 57

Trp

Hint 57

W

Front 58

Tyrosine

Back 58

Tyr

Hint 58

Y

Front 59

Valine

Back 59

Val

Hint 59

V

Front 60

Hydrophobic (apolar) R-groups

Back 60

Reside predominantly in the interior of proteins, involved in protein folding.
Do not ionize nor participate in formation of H-bonds

Front 61

Hydrophillic (polar) R-groups

Back 61

Bonds primarily reside in the exterior surfaces of proteins

Front 62

Buffers

Back 62

Solutions that minimize a change in [H+] or pH when an acid or base is added.

Front 63

Isoelectric point (pI)

Back 63

pH at which an amino acid has no net charge; least soluble at this pH

Front 64

Apolar proteins (aliphatic and aromatic amino groups) are...

Back 64

insoluble in water and more soluble in cell membranes.

Front 65

Proteins rich in polar amino acids are...

Back 65

water soluble

Front 66

Proteins rich in basic side chains (Lys, Arg) are...

Back 66

positively charged at neutral pH

Front 67

Proteins rich in acidic side chains (Glu, Asp) are...

Back 67

negatively charged at neutral pH