Biochemistry, First Exam

Front 1

What do most of the functional groups contain?

Back 1

oxygen and nitrogen, among the most electronegative elements

Front 2

What functional groups does ATP contain?

Back 2

esters and anhydrides involving a phosphoric acid

Front 3

What is an ionic bond, and what is an example?

Back 3

complete transfer of electrons from one ion to another making them oppositely attracted, NaCl

Front 4

What is a covalent bond and what is an example?

Back 4

it is the sharing of electrons. carbon dioxide molecule, H molecule, carbon tetraflouride

Front 5

What is meant by electronegativity?

Back 5

the mathematical parameter of which an atom attracts electrons in its bond with another atom

Front 6

What is the most electronegative atom?

Back 6

flourine(4)

Front 7

What are some high electronegative atoms?

Back 7

oxygen (3.5) and nitrogen (3)

Front 8

What is an nonpolar bond?

Back 8

covalent bond that has even distribution of electron density, ex H molecule, and oxygen

Front 9

Which molecule has a slight difference in electronegativity?

Back 9

methane, nonpolar still

Front 10

What is a polar bond?

Back 10

covalent bond with uneven distribution of electrons, water is an example

Front 11

How is polarity of a molecule defined?

Back 11

the electronegativity of atoms, and the geometry of the bonds

Front 12

What is true about a polar bond and a polar molecule?

Back 12

They are both dipoles

Front 13

What macromolecules can be found in a cell?

Back 13

lipids, nucleic acids, amino acids, carbs

Front 14

What ions can be found in a cell?

Back 14

Na Ca K Mg

Front 15

What causes Menkes' syndrome?

Back 15

too LITTLE copper,

Front 16

What are some symptoms of Menkes syndrome?

Back 16

sparse kinky hair, physical retardation, deterioration of the brain

Front 17

What is the kay fleisher ring seen in? and what causes it?

Back 17

Wilsons disease, too MUCH copper

Front 18

What disease is characterized by tremors, trouble swallowing, and slurred speech?

Back 18

Wilsons disease, MUCH copper

Front 19

What is endemic goiter caused by?

Back 19

iodine deficiency

Front 20

What diseases are caused by iodine deficiency?

Back 20

endemic goiter, dwarfism, mental retardation

Front 21

Describe what would happen with too little or too much iron.

Back 21

Too MUCH= hemachromatosis, > liver CA
too LITTLE=anemia

Front 22

Why does biochem use the methods and concepts of ochem?

Back 22

because they deal with carbon based compounds

Front 23

What is an example of how functional groups influence biological activity?

Back 23

Steroids. A diff fxnl group attached the same organic molecule changes its fxn,

Front 24

What does alpha alanine have attached to it?

Back 24

carboxylic acid and an amide

Front 25

What is acetyl coenzyme A?

Back 25

intermediate in the oxidation of carbs, lipids, and proteins.

Front 26

What percentage of the body is water?

Back 26

55-60%

Front 27

What portion of the fluid in the body is extracellular?

Back 27

2/3

Front 28

What are some examples of hydrophilic compounds?

Back 28

they contain ionic or polar bonds. and ex are ketones, acetone, sugars, alcohols, ionic compounds, amino acids, and phosphate esters

Front 29

Are hydrocarbons hydrophilic or hydrophobic?

Back 29

hydrophobic (ie gasoline)

Front 30

Describe the water solubility principle.

Back 30

Like dissolves like. The positive dipole of water attracts the negative ion of another molecule

Front 31

What are the two types of interactions with water?

Back 31

ion-dipole (ex. KCl) and dipole-dipole (ex. alcohol)

Front 32

What is an amphipathic molecule?

Back 32

partially hydrophobic and hydrophilic molecule

Front 33

Define the hydrophobic effect.

Back 33

tendency of nonpolar groups in water to self associate to minimize contact with the polar solvent

Front 34

How are micelles and bilayers created? What is the difference between them?

Back 34

hydrophobic effect, the hydrophobic parts of an amphipathic molecule are buried, and the hydrophilic heads are free in contact with water. Micelle is a spherical arrangement, and bilayer is..a bilayer.

Front 35

What is most commonly the hydrogen bond acceptor in molecules?

Back 35

electronegative atoms, so O and N.

Remember.Hydrogen bond is different than a covalent bond to hydrogen.
Water molecules are held together by hydrogen bonds

Front 36

What are some examples of important biological H bonds?

Back 36

H bonds in water.
Bonding of water to other molecules.
Protein and nucleic acid structures.

Front 37

What is H bonds influence in nucleic acids?

Back 37

base pairing

Front 38

What is H bonds influence in proteins?

Back 38

H bonds between N-H and O=C determine different conformations. (alpha helix, beta strand, hairpin)

Front 39

Define acid and define base.

Back 39

Acid - Donates protons

Base- Accepts protons

Front 40

What are the conjugate acid-base pairs?

Back 40

HA, A-, B+, BOH

Front 41

What is Ka?

Back 41

the dissociation constant. refers to acids. The higher the Ka, the stronger the acid, the more protons donated to solution.

Front 42

Remember:

Back 42

Water is both a weak acid and a weak base

Front 43

Define pH

Back 43

a mathematical parameter that measures the acid/base character of an
aqueous solution by expressing conveniently its hydrogen ion concentration
pH = -log10 [H3O+] = -lg [H+]

Front 44

Describe the difference in structure between cortisol and aldosterone.

Back 44

Cortisol has 3 hydroxyl groups, and aldosterone only has 2

Front 45

Describe the difference in structure between progesterone and testosterone

Back 45

Progesterone has a ketone group (not on benzyl ring) and testosterone has a hydroxyl group

Front 46

What is the difference between glucose and fructose?

Back 46

glucose=not so sweet aldehyde
fructose- very sweet ketone

Front 47

What are the three different ways amphipathic molecules can arrange in water?

Back 47

micelles, bilayers, clusters

Front 48

What is stereochemistry?

Back 48

the study of the 3d structure of molecules.

Front 49

What are isomers?

Back 49

different compounds with the same molecular formula

Front 50

What is a constitutional isomer?

Back 50

compounds that have the same molecular formula but with different connectivities

Front 51

What are stereoisomers?

Back 51

compounds with the same connectivity but different arrangements in space

Front 52

What are enantiomers?

Back 52

stereoisomers that are mirror images of eachother but not superimposable

Front 53

What are diastereomers?

Back 53

stereoisomers that are not mirror images of eachother

Front 54

What are geometric isomers? and what are some examples?

Back 54

they are isomers that are determined by the restriction of rotation about a double bond .
maleic acid=cis
fumaric acid=trans

Front 55

Is an achiral a superimposable image?

Back 55

yes

Front 56

What is a racemic mixture?

Back 56

contains both R and S enantiomers
r=clockwise
s=counter

Front 57

What does stereospecific mean?

Back 57

complementary configuration and conformation
ex.
enzyme-substrate
hormone-receptor
antigen-antibody

Front 58

How can humans distinguish enatiomers?

Back 58

smell and taste (they are chiral)

Front 59

What portion of thalidomide produced negative effects?

Back 59

S thalidomide

Front 60

What are some examples of enantiomer drugs?

Back 60

Ketoprofan (R=toxic, S=analgesic,anti-inflam)
Fluoxetine (S=prevents migraines, RS=prozac)
Dopa (L=antiparkinsons, D=inactive)

Front 61

Name some peptide hormones.

Back 61

oxytocin, vasopressin, carnosine

Front 62

What is carnosines role in the body?

Back 62

present in muscle and brain tissue. powerful antioxidant

Front 63

What is a peptide bond?

Back 63

joining of two amino acids by eliminating water and between the carboxyl group of one acid and the amino group of another

Front 64

Name the basic amino acids.

Back 64

positive=basic
HAL- histidine, arginine,lysine

Front 65

Name the essential amino acids.

Back 65

Any Help In Learning These Little Molecules Proves Truly Valuable. Arginine, Histidine, Isoleucine, Leucine, Threonine, Lysine, Methionine, Phenylalanine, Tryptophan, Valine

Front 66

Name the nonpolar amino acids.

Back 66

AVL IPM PT
Alanine, Valine, Leucine, Isoleucine, Proline, Methionine, Phenylalaine, Tryptophan

Front 67

Define uncommon amino acids.

Back 67

produced by common amino acids by posttranslational modification

Front 68

What is the amino acid precursor for melatonin?

Back 68

Tryptophan

Front 69

What is arginine a precursor for?

Back 69

polyamines,
dna synthesis and cell growth and ion modulaters

Front 70

What foods can you receive essential amino acids from?

Back 70

eggs, yogurts, meat, cheese, beans

Front 71

What does amphoteric mean?

Back 71

ability to act as a base and acid
(water, amino acids)

Front 72

What is the blood pH?

Back 72

7.35-7.45

Front 73

What are the homeostatic buffer systems?

Back 73

-bicarbonate-blood
-phosphate-buffer cells
-proteins -blood through red cells

Front 74

What are disulfide bonds in?

Back 74

oxytocin and vasopressin

Front 75

What are in peptide bonds?

Back 75

O=C and N-H

Front 76

What do the negatively charged amino acid side chains have?

Back 76

ionized carboxyl groups

Front 77

What is dopamines precursor?

Back 77

L tyrosine

Front 78

What can constiutional isomers yield as different compounds?

Back 78

different functional groups
different positions of functional groups
different carbon skeleton

Front 79

What is a biologically important geometric isomer?

Back 79

Vit A

Front 80

What is special about enantiomers?

Back 80

They have the same physical and chemical properties but different biological and optical ones

Front 81

What are some biologically important constitutional isomers?

Back 81

glucose and fructose

Front 82

What is an amino acid?

Back 82

a compound that contain both an amino group and a carboxyl group
bound to the same carbon atom.

Front 83

What are the examples of uncommon amino acids?

Back 83

Thyroid hormones t3 and t4 (thyroxine)

Front 84

What is the precursor for catecholamines?

Back 84

amino acid tyrosine

Front 85

What is the difference between amphoteric/amphiprotic and amphipathic?

Back 85

amphipathic is having both hydrophilic and hydrophobic ends. amphoteric is the ability to act as both an acid and a base

Front 86

What is carnosine?

Back 86

naturally occuring dipeptide in muscle and brain tissue. also an antioxidant

Front 87

What are the macromolecules found in cells?

Back 87

lipids nucleic acids proteins and carbs

Front 88

What are 96% of all living things composed of?

Back 88

O C H N

Front 89

What are the most common covalent bonds?

Back 89

Monovalent (H), Divalent (O), trivalent (N), tetravalent (C)

Front 90

What are polar molecules or polar bonds known as?

Back 90

dipoles

Front 91

How is NaCl dissolved in h20?

Back 91

ion-dipole reaction

Front 92

Define a hydrogen bond

Back 92

particular case of attractive force between dipoles. most likely O or N when they have a lone pair or when H is covalently bonded to an electronegative atom