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Chemistry > 2cd Exam > Flashcards

2cd Exam Flashcards

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1
Q

Carbon always has how many bonds total

A

Four

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2
Q

Carbon can receive and donate

A

Electrons

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3
Q

Alkanes

A

Completely saturated with hydrogens, single bond

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4
Q

Hydrocarbons

A

Hydrogen and carbon, saturation of hydrocarbons refers with only single bonds between carbons and are saturated with hydrogen

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5
Q

Alkenes

A

Have a set of carbons with a double bond and are NOT saturated w carbon

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6
Q

Alkynes

A

Have at least one set of triple bonds are NOT saturated with carbon

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7
Q

Aromatic rings

A

Six carbons with alternating double bonds one hydrogen, base ring with hydrogen only called a benzene

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8
Q

Substitutions in places of the hydrogen atoms with…

A

Hydroxyl groups (OH) constitutes alcohol

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9
Q

Alkanes name methane

A

Methanol had 1 carbon atom

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10
Q

Alkanes name ethane

A

Ethanol 2 carbon atoms

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11
Q

Alkanes name propane

A

Propanol has 3 Carbon atoms

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12
Q

Alkanes name butane

A

Butane 4 carbon atoms

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13
Q

Isomer

A

Same molecular formula but different chemical structure: same number of atoms but different arrangement, especially true of organic

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14
Q

Two types of isomers

A

Structural and stereoisomers

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15
Q

Chiral

A

4 different groups attached

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16
Q

Single bonds between carbons allow rotation along axis

A

Trans opposite side

Cis is same side

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17
Q

Animals fats

A

Cis isomers naturally
Solid at room temp
Unsaturated = cis

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18
Q

Vegetable oils

A

Some trans form

Liquid room temp

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19
Q

Carbonyl groups in aldehydes and ketones

A

Are oxygen atoms attached to carbon atoms w a double bond

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20
Q

L isomers of amino acids and D isomers of sugars

A

Are the only ones animals can utilize and form glucose

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21
Q

Enzymes convert acetaldehyde into

A

Acetic acid or it’s ionized salt form acetate

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22
Q

Amines

A

Organic derivatives of ammonia (NH3), substituting one or more hydrogens with an akyl (R) group or an aromatic group

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23
Q

Primary amine

A

One R group

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24
Q

Secondary amine class

A

Two r groups

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25
Q

Tertiary amine group

A

Three r groups

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26
Q

Ammonia mixed with water

A

Steal hydrogen from water forming an ammonium action and hydroxide anion. Mixed w acid ammonia will Take a hydrogen and form a SALT with acid anion. Ammonia acts like a base

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27
Q

Most important quaternary amine in body

A

Choline

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28
Q

One of Most important neurotransmitter in body

A

Acetylcholine

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29
Q

What breaks up Esther bonds

A

Hydrolysis

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30
Q

Tyr

A

Tyrosine and it’s neurotransmitter is Epinephrine

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31
Q

Trp

A

Tryptophan and it’s neurotransmitter is serotonin

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32
Q

His

A

Histidine and it’s neurotransmitter is histamine

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33
Q

Nearly every carbohydrate

A

Every carbon has one hydrogen and one hydroxyl on two of the bonds, exception one carbon will
Be part of hydroxyl group

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34
Q

Carbohydrate functions

A

Source of fuel, synthesis of cellular components, storage, make glycoproteins and nucleus acids

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35
Q

Simple oxidation

A

Incomplete and inefficient

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36
Q

Biological oxidation.

A

Complete oxidation and more efficient

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37
Q

Smallest and simplest carbohydrate

A

Three carbon glyceraldehyde

The second carbon is chiral

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38
Q

Most carbohydrates are at least

A

5 or more typically 6 carbons long.

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39
Q

Chiral carbon

A

Second to the last

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40
Q

Monosaccharides

A

One sugar

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41
Q

D ribose

A

Pentose

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42
Q

D glucose

A

Hexose

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43
Q

D galactose

A

Hexose

44
Q

D fructose

A

Hexose

45
Q

Most stable form of these 5 and 6 carbon monosaccharides are

A

Cyclic

46
Q

Disaccharides and 3 significant

A

Monosaccharides bonded by oxygen

Sucrose, lactose, maltose

47
Q

Starch

A

Polymer consisting entirely of D glucose units.

48
Q

Amylose

A

Starch made up

Of long unbranched chains of D glucose

49
Q

Glycogen

A

Animal form of polymerized D glucose

50
Q

Most abundant polysaccharide in nature and most important structural polysaccharide in plant kingdom

A

Cellulose

51
Q

Complex carbohydrates

A

Longer and more branched and have a slower rate of digestion and absorption of glucose from the intestine

Of vegetables function as slow sugars

52
Q

Fatty acids

A

Donate hydrogen in aqueous solutions

Carboxylic acid ionized group at one end and a zig zag line representing carbons

53
Q

Micelles

A

Formed from small droplets of oil mix w water

Phospholipid enclosed in water

54
Q

Free fatty acids are usually

In the form

A

Of salts with cations at physiological pH

55
Q

Fatty acids characteristics

A

Carbons and hydrogen only attach to carboxylic group, come in pairs usually 10-20 carbons in length, even number

56
Q

Alpha carbon

A

First carbon after the carboxylic acid carbon

57
Q

Beta carbon is

A

the carbon age alpha, where oxidation of the fatty acid occurs

58
Q

Omega carbon

A

LAST carbon

59
Q

Fatty acids chains can be

A

Saturated and unsaturated

60
Q

Essential fatty acids

A

Body needs them and can not make them

61
Q

2 essential fatty acids

A 
Linolenic acid (omega 6)
Linolenic acid (omega 3)
62
Q

Double bonds cause what In chains of fatty acids

A

Kinks, which keep fatty acids from packing together too tightly

63
Q

Triglycerides

A

Most common storage form of fatty acids
They will not form micelles alone because they have no polar ends unlike free fatty acids
They will not mix with water alone

64
Q

Esterification

A

Process of linking an acid to an alcohol which yields a water molecule
Reverse process hydrolysis

65
Q

Phospholipids

A

Diverse group of functional and structural lipids

66
Q

To identify a phospholipid

A

Hydrophilic/ polar head and two hydrophobic tails (fatty acid chains) one with a kink

67
Q

Steroids are

A

Usually grouped with lipids and are NOT fatty acids or triglycerides
Cyclic acids
Soluble in lipids, limited solubility
17 carbons in 4 rings

68
Q

Lipid bi layer

A

Cell membrane and structural backbone

69
Q

Arachidonic acid

A

20 carbon fatty acid that is converted by an enzyme called COX

70
Q

Arachidonic acid converted by COX into

A

Prostaglandin

71
Q

Amino acids

A

Proteins composed of chains or polymers of amino acids bonded together
20 different common Found

72
Q

Cysteine

A

An amino acid that contains a sulfydryl group to form a disulfide bond

73
Q

Which kind of bond is formed between two sulfur atoms

A

Covalent

74
Q

Linking of amino acids

A

Peptide bonds, water is given off as the bond is formed

75
Q

Polarized portions of amino acids are attracted

A

To those of opposite polarity

76
Q

Functions of proteins

A

Catalytic, structural, storage, protective, regulation, nerve impulses, movement, transport, energy

77
Q

Primary structure of protein

A

A chain of amino acids, specific ones, order, length

78
Q

When proteins are exposed and o chemical or physical conditions that disrupt protein structure

A

Denaturation

79
Q

Four levels of protein structure

A

Primary, secondary, tertiary, quaternary

80
Q

Chemical that facilitates and speeds up chemical reaction without being consumed by reaction

A

Catalyst

81
Q

Protein structures the increase chemical reactions in the body which allow life to exist

A

Enzymes

82
Q

Oxidoreductases

A

Oxidation reduction reactions

83
Q

Transferases

A

Transfer functional groups

84
Q

Lyases

A

Formation or removal of a double bond w group transfer

85
Q

Isomerases

A

Convert molecule from one isomer to another

86
Q

Ligases

A

Formation of new bonds, joining groups with ATP usage

87
Q

Cofactors

A

Assist enzymes are non protein sometimes non organic and even ionic

88
Q

Coenzymes

A

Assist enzymes and are

Organic

89
Q

Binding of the substrate to the enzyme site is by

A

Hydrophobic attraction, hydrogen bonding, and or ionic bonding

90
Q

Lock and key model

A

Key is for substrate and lock is for enzyme

91
Q

Allosteric regulation

A

Feedback loop, amount of final product will

Influence the degree of inhibition

92
Q

Genetic control

A

Protein production including enzymes is under control

Of genetic material

93
Q

Enzymes reside

A

Inside cells and are released only

In quantity when cells are damaged or die

94
Q

Enzyme alkaline phosphatase

A

Organ of pathology liver or bone

95
Q

Enzyme amylase

A

Organ of pathology pancreas

96
Q

Enzyme CPK

A

Organ of pathology heart

97
Q

Enzyme AST

A

Organ of pathology Liver and or heart

98
Q

Enzyme ALT

A

Organ of pathology liver

99
Q

Enzyme LDH

A

Organ of pathology heart and or liver

100
Q

Enzyme lipase

A

Organ of pathology pancreas

101
Q

Enzyme lysozyme

A

Organ of pathology unique to leukemia

102
Q

Someone overdoes with Tylenol would injury liver, what enzymes should be monitored

A

AST AND ALT levels and repeated over time would show recovery or worsening of liver

103
Q

Methanal

A

Formaldehyde

2 carbons

104
Q

Ethanal

A

Acetaldehyde

2 carbons

105
Q

Propane

A

Acetone
Ketone

3 carbon

106
Q

Butanone

A

Methyl ethyl ketone
Ketone

3 carbon

Chemistry (5 decks)

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