Biochem Review Week 1

Front 1

The catabolic pathways of fuel metabolism produce energy todrive?

Back 1

Anabolic pathways and other energy-requiring physiological processes

Front 2

The energy to make ATP comes fromthe __ of carbon atoms

Loss of electrons is?

Gain of electrons is?

Back 2

Oxidation of carbon atoms

Loss of electrons = oxidation

Gain of electrons = reduction

Front 3

Asaturated carbon oxidized to an unsaturated carbon makes how many ATP?

An alcohol oxidized to an aldehydeor ketone can make how many ATP?

An alcohol oxidized to a carboxylicacid can make how many ATP?

Everyone of these reactions removeshow many electrons and hydrogen?

Back 3

saturated--> unsaturated: 2 ATP

alcohol--> aldehyde/ketone: 3 ATP

alcohol --> carboxylic acid: 4 ATP

All remove 2 e- and 2 H+

Front 4

What is a covalent bond?

What are the 6 atoms that form covalent bonds?

Back 4

A pair of electrons shared by 2 atoms

-Carbon

-Hydrogen

-Oxygen

-Nitrogen

-Sulfur

-Phosphorus

Front 5

Valence is the number of bondsformed by an atom

What is the valence of Hydrogen?

Carbon?

Oxygen?

Nitrogen?

Sulfur?

Phosphorus?

Back 5

Front 6

What is the most electronegative atom?

Whatis the least most electronegative atom?

Back 6

Front 7

N, S, and O have non bonded electron pairs

Nin NH3 has a tendency to __ a hydrogen atom

Oin a water molecule has a tendency to __ a hydrogen atom

Back 7

N in NH3 has a tendency to capture a hydrogen atom

O in a water molecule has a tendency to release a hydrogen atom (more electronegative)

Front 8

Whatis resonance?

What stabilizes the resonantstructure?

Back 8

Sharing of e- between 3 or more atoms

Delocalization stabilizes resonant structure

Front 9

Which is the most stable in the cell?

Back 9

Front 10

Back 10

Front 11

Back 11

Front 12

Back 12

Front 13

Are what type of bonds?

Back 13

Non covalent bonds

Front 14

Strength of hydrogen bond (H atom inpolar covalent bond and unpaired e-) is dependent on what 2 things?

Electrostatic/Ionic (force between+ and – atoms) bond dependson?

Hydrophobic bonds push non polarmolecules together because they preferto associate with water molecules

Back 14

Distance and orientation

Distance only

Front 15

What is the proton donor?

Whatis the proton acceptor

Back 15

Acid = proton donor

Base = proton acceptor

Front 16

describe the equation

Back 16

AH = acid

A = base

Front 17

What is the universal medium of proton exchange?

Back 17

Water = can act as an acid or base

Front 18

Watercan donate a proton to itselfWhat is the water constant Kw?

Back 18

Front 19

What is the definition of pH?

High pH means?

Lower pH means?

Back 19

pH = -log[H+]

High pH = low H concentration

Low pH = high H concentration

Front 20

Ka = aciddissociation constant

Ka isthe H+ concentration at which exactly half of A is protonated

What does it mean if Ka=H+

Back 20

Front 21

pKa= ?

Back 21

pKa = -logKa

Front 22

What does it mean when pH = pKa?

Back 22

Half of A is unprotonated and the other half is protonated

Front 23

WhenpH is one unit higher than pKa whatdoes this mean?

When pH is one unit lower than pKa, what does this mean?

Back 23

High pH = low H concentration = favors dissociation, so more than half of A will be dissociated

Low pH = high H concentration = favors protonation, so more than half will be protonated

Front 24

Eachmolecule spends half its time as COOH and half as COO-, so it has a averagednet charge of?

Back 24

Front 25

Buffers work well when the pH is near?

What is the most importantphysiological buffer?

How does bicarbonate evaporate acidity?

Back 25

pH is near their pKa

buffers are weak acids or weak bases

Bicarbonate

The bicarbonate buffer system allows the body to convert H+ from metabolic acids into gaseous CO2 that can be exhaled

Front 26

What is a peptide bond?

Becauseof resonance, peptide bonds have a partial double bond character making them?

Back 26

Connects amino acid by joining the carboxyl groupof each amino acid to the alpha amino group of the adjacent amino acid

Planar and rigid

Front 27

How many amino acids are necessary for the minimum size of asmall enzyme for catalytic activity

Back 27

120 amino acids

Front 28

primary structure

secondary structure

tertiary structure

quaternary structure

Myoglobin is what structure?

Hemoglobin is what structure?

Back 28

1=polypeptide chain

2=alpha helices with repeated organized conformation

3=secondary structures combined

4=subunit structure

Myoglobin = tertiary

Hemoglobin = quaternary

Front 29

Primary structure is held together by?

Thefolded structures of Secondary, tertiary, and quaternary is held together by?

Secondarystructures like the alpha helix or beta sheet are held together by what bonds?

Back 29

Covalent

Non-covalent

Hydrogen bonds between the C=O and N-H atoms of peptide bonds

Front 30

Collagen chains associate into?

Which is what kind of structure?

Onlypolypeptides with __ at everythird position in amino acid sequence can forma this

Back 30

Triple Helixes

Secondary

Glycine

Front 31

Thefolding elements of a secondarystructure to form a tertiary structure includewhat 4 bonds?

Back 31

1. ionic bonds

2. hydrogen bonds

3. hydrophobic bonds (most important)

4. disulfide bonds (only outside the cell

Front 32

Saliva has a protective effect on dental enamel, why?

Alcohol can result in vomiting and dehydration, how doesthis affect bicarbonate and saliva?

When you hyperventilate, what happens to the pH?

Hypoventilation causes pH to?

Back 32

Bicarbonate in saliva is a protective adaptive response that reduces the acidity in the mouth

Bicarbonate cannot buffer the strong stomach acid to protect teeth and dehydration means less saliva=less bicarbonate

Hyperventilate=pH goes up and alkanizes blood (due to CO2 depletion)

Hypoventilate = pH goes down (CO2 goes up) - holding your breath

Front 33

Back 33

Front 34

Back 34

Front 35

Back 35

Front 36

pH of 7.4?

Back 36

Higher pH = less H = -1

Lower pH = more H = +1

Higher pH = less H = -1

Overall net charge = -1