Organic Chemistry Flashcards

1
Q

What is the backbone of all Organic Chemistry called

A

Carbon Skeleton

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2
Q

What are the 4 major categories of organic macromolecules

A

1) Carbohydrates
2) Lipids
3) Proteins
4) Nucleic Acids

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3
Q

What are the 4 main elements in organic molecules/compounds

A

Carbon
Hydrogen
Oxygen
Nitrogen

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4
Q

What type of bonds hold organic compounds together

A

Covalent (mainly)

Hydrogen (sometimes)

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5
Q

What shape does Glucose form

A

Hexagon

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6
Q

What are the carbons in the skeleton that bind to hydrogen called

A

Hydrocarbons

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7
Q

What are the 7 main Functional Groups

A

1) Hydroxyl
2) Sulfhydryl
3) Carbonyl
4) Carboxyl
5) Ester
6) Phosphate
7) Amino

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8
Q

Characteristics of Hydroxyl Group

A

Contains OH
Polar/Hydrophilic
Ex Alcohol

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9
Q

Characteristics of Sulfhydryl Group

A

Contains SH group

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10
Q

Characteristics of Carbonyl Group

A

Keytones and Aldehydes

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11
Q

Characteristics of Carboxyl Group

A

Contains COOH
Component of Amino Acids
Can act as an acid

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12
Q

Characteristics of Ester Group

A

Compounds found in fats, oils and triglycerides

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13
Q

Characteristics of Phosphate Group

A

Contains PO4

Key component of ATP

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14
Q

Characteristics of Amino Group

A

Contains NH2
Component of Amino Acids
Can act as a base (NH3)

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15
Q

What does the “R” signify

A

Variable group

What the Functional Group is attached to

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16
Q

Define Monomer

A

Smallest unit of an organic molecule

Ex Glucose

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17
Q

Define Polymer

A

Larger organic molecule consisting of monomers
*Usually created by dehydration synthesis
Ex Glycogen

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18
Q

Define Isomer

A

Molecules with same chemical formula but different chemical structure
*Functional group is attached to different Carbon #s

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19
Q

Example of an Isomer

A

Glucose and Fructose

*Reversible Reaction

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20
Q

How does a Dehydration reaction effect Peptide Bonds

A

Removes water to form peptide bonds

Ex Glucose + Fructose = Sucrose + H2O

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21
Q

How does a Hydrolysis reaction effect Peptide Bonds

A

Add water to break peptide bonds

Ex Sucrose + H2O = Glucose + Fructose

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22
Q

Which Elements make up Carbohydrates

A

Carbon
Oxygen
Hydrogen

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23
Q

Define Carbohydrate

A

Carbon molecules that are saturated with Hydrogen and Oxygen

*Watered /Hydrated Carbons!

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24
Q

What suffix do most carbohydrates end with

A

“Ose”

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25
Q

What are the 3 Classifications of Carbohydrates

A

Monosaccharides
Disaccharides
Polysaccharides

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26
Q

What is the monomer of Charbohydrates

A

Monosaccharides

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27
Q

Examples of Monosaccharides

A

Glucose, Fructose, Gelactose, Ribose, Deoxyribose

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28
Q

What is a Disaccharide

A

Product of 2 or more monosaccharides by dehydration synthesis
Ex Glucose + Fructose = Sucrose (disaccharide) + H2O

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29
Q

What is a polysaccharide

A

Up to thousands of monosaccharides combined together

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30
Q

3 Examples of Polysaccharides

A

Glycogen
Starches
Cellulose

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31
Q

What is Glycogenolysis

A

Breakdown of Glycogen into Glucose

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32
Q

What is Glycolysis

A

Breakdown of Glucose into smaller components to make ATP

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33
Q

What is Glycogenesis

A

The making of Glycogen from Glucose

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34
Q

What percentage of our body is made up of Carbohydrates

A

Less than 3%

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35
Q

Characteristics of Lipids

A

Less oxygen to hydrogen ratio
More non-polar/hydrophobic
Do not dissolve easily in water

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36
Q

What lipids will dissolve in Water (3)

A

Very small ones
Glyco-lipids (sugar-fats)
Lipo-proteins (fat-proteins)

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37
Q

What are the 6 Classifications of Lipids

A

1) Fatty Acids
2) Triglycerides
3) Phospholipds
4) Steroids
5) Eicosanoids
6) Other

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38
Q

What are Fatty Acids

A
Simplest lipid (not a monomer)
Consist of a Carboxyl group and a Hydrocarbon Chain
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39
Q

What is a Saturated Fatty Acid

A

All Carbons on the chain are fully saturated with Hydrogen

*Single covalent bonds only

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40
Q

What is an Unsaturated Fatty Acid

A

A fatty acid with 1 or more double covalent bonds

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41
Q

What is a Monounsaturated Fatty Acid

A

Fatty acid with 1 double covalent bond (1 kink)

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42
Q

What is a Polyunsaturated Fatty Acid

A

Fatty acid with 2 or more double covalent bonds (2+ kinks)

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43
Q

What are Triglycerides

A

Contain 1 Glycerol molecule and 3 Fatty Acids chains
aka Triglycerols
Formed by Dehydration Synthesis
*Unlimited ability to be stored in adipose tissue in certain areas of the body

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44
Q

Difference between Oils and Fats

A

Fats: tend to be Saturated Fats - solid at room temperature
Oils: tend to be Unsaturated Fats - liquid at room temp

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45
Q

What type of fats are better for us and why

A

Polyunsaturated Fats

More Covalent Bonds = Less Hydrogen = easier for body to metabolize and incorporate into our tissues

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46
Q

What are Essential Fatty Acids

A

FA’s that our body cannot produce itself and therefore but be ingested
Ex Omega-3, Omega-6

47
Q

What are Non-Essential Fatty Acids

A

FA’s produced by our body

Ex Omega-9

48
Q

What is Hydrogenation

A

When Cis FA’s are processed to become Trans FA’s

49
Q

Difference between Cis and Trans FA’s

A
Cis = Hydrogens on same side of double covalent bond
Trans = Hydrogens on opposite sides of the bond
50
Q

What are the 2 Lipoproteins of Cholesterol

A
LDL = Low Density Lipoprotein
HDL = High Density Lipoprotein
51
Q

Which type of Cholesterol is the “bad” one

A

LDL

52
Q

Characteristics of Phospholipids

A

Contains Phosphorous in its structure
Major components of cell membranes
Amphipathic

53
Q

Define Amphipathic

A

Molecule with a Polar end AND a non-polar end

54
Q

Characteristics of Steroids

A

4 Rings of Carbon

55
Q

Examples of Steroids in the body (4)

A

Hormones
Cholesterol
Bile Salts
Vitamin D

56
Q

Characteristics of Eicosanoids

A

20 Carbon FA chains

Involved in inflammatory responses

57
Q

2 Types of Eicosanoids

A

Prostaglandins

Leukotrienes

58
Q

What are classified as “Other” fats

A

Carotenes
Vitamin E
Vitamin K

59
Q

What Percentage of our body is made up of Proteins

A

12-18%

60
Q

6 Types of Proteins found in the body

A

1) Structural
2) Regulatory
3) Contractile
4) Immunological
5) Transport
6) Catalytic

61
Q

Function of Structural Proteins

A

Key role in formation and function of cells/tissues

Ex Keratin in skin, hair, and nails

62
Q

Function of Regulatory Proteins

A

Key parts of the structure of hormones

Ex Insulin

63
Q

Function of Contractile Proteins

A

Filaments in muscles (myocin) and cellular components (actin)

64
Q

Function of Immunological Proteins

A

Ex White Blood Cells, Antibodies

65
Q

Function of Transport Proteins

A

Key component of red blood cells and membrane structures of certain cells
Ex Hemoglobin - Transporting oxygen

66
Q

Function of Catalytic Proteins

A

Forms majority of enzymes found in the body

67
Q

What are the Monomers of Proteins

A

Amino Acids

68
Q

What are the components of an Amino Acid

A
Carboxyl Group (acid)
Amine Group (base)
Side Chain
69
Q

How many Amino Acids are there

A

20

70
Q

How many Amino Acids are Non-Essential

A

12

71
Q

What Joins Amino Acids together to form Proteins

A

Peptide Bonds

72
Q

What is a Peptide Bond

A

Type of Covalent Bond formed through Dehydration Synthesis

Bond between the N (of the NH2) of one amino acid and the C of the Carboxly Group (COOH) on another

73
Q

What is the Creation of Proteins called

A

Protein Synthesis

74
Q

What is a Dipeptide

A

2 Amino Acids (aa), 1 Peptide Bond

75
Q

What is a Polypeptide

A

10-2000+ Peptides

76
Q

What are the 4 Structural Types of Proteins

A

1) Primary
2) Secondary
3) Tertiary
4) Quaternary

77
Q

Primary Structure of a Protein

A

Unique sequence of amino-acids in a polypeptide chain

*Genetically determined

78
Q

Secondary Structure of a Protein

A

Repeated twisting and/or folding of neighbouring amino-acids in a polypeptide chain
Stabilized by Hydrogen Bonds
Ex Beta Pleated Sheets, Alpha Helices, or both

79
Q

Tertiary Structure of a Protein

A

3D shape of the polypeptide chain

Secondary structures folding in on themselves

80
Q

Quaternary Structure of a Protein

A

Arrangement of 2 or more polypeptide chains

Ex Hemoglobin

81
Q

What is Denaturation

A

Altering or destruction of a protein

82
Q

What are the 2 Components of an Enzyme

A

Apoenzyme (Protein Portion)

Cofactor (Non-Protein)

83
Q

What are Enzymes

A

Protein molecules that act as catalysts in biochemical reactions

84
Q

What makes Enzymes Highly Specific

A

Their Active Site only binds to certain Substrates

85
Q

What are the 3 Components of a Nucleotide

A
Nitrogen Base
Pentose Sugar (5-Carbon Sugar)
Phosphate Group (PO4)
86
Q

Where are Nucleic Acids found

A

Inside the nucleus of cells

87
Q

What are the 5 Nitrogenous Bases

A

1) Thymine
2) Guanine
3) Cytosine
4) Adenine
5) Uracil

88
Q

What are the 2 Types of Nucleic Acids

A
Ribonucleic Acid (RNA)
Deoxyribonucleic Acid (DNA)
89
Q

Function of DNA

A

“Blue Print”
Forms the genetic material (chromosomes)
Present in all of our cells

90
Q

Describe what DNA does

A

Consists of genes (segments of DNA molecule) that consist of specific Nucleotides which decide the combinations of Amino Acids to produce proteins. These proteins group together to form larger proteins that become functional and can be passed on as traits from one generation to the next

91
Q

Characteristics of DNA

A

Double Stranded
Sugar = Deoxyribose
Nitrogenous Bases = Thymine, Adenine, Cytosine, Guanine

92
Q

How is the Double Helix of DNA formed

A

Sides are formed by alternating sugar and phosphate
Rungs are formed by nucleotides (alternating Pyrimidines and Purines)
*Hydrogen bonds between bases

93
Q

What are the Monomers of Nucleic Acids

A

Nucleotides

94
Q

Which bases make up the Pyrimidines

A

Cytosine, Thymine, Uracil

95
Q

Which bases make up the Purines

A

Adenine, Guanine

96
Q

Which bases pair up in DNA

A

Adenine and Thymine
Cytosine and Guanine
*AT Cricket Ground

97
Q

Function of RNA

A

Relays instructions from the genes to guide the cell’s protein synthesis

98
Q

Characteristics of RNA

A

Single Strand
Sugar = Ribose
Bases = Adenine, Guanine, Uracil, Cytosine

99
Q

3 Types of RNA found in the Cell

A

1) Messenger
2) Transfer
3) Ribosomal

100
Q

What do Messenger RNA do

A

Transcribe original DNA

101
Q

What do Transfer RNA do

A

Amino acid translation

102
Q

What do Ribosomal RNA do

A

Forms template for amino acid translation

103
Q

What is ATP

A

Adenosine Triphosphate

104
Q

Function of ATP

A

Energy

Necessary for all reactions that occur in our body

105
Q

Components of ATP (3)

A

1 Adenine
Phosphate Group
1 Ribose Sugar

106
Q

What is ADP and how is it made

A

Adenosine Di-phosphate

1 phosphate is liberated from ATP

107
Q

How does ATP Produce Energy

A

The energy produced when ATP becomes ADP (exergonic reaction from the breaking of the bond between phosphate groups)

108
Q

What type of reaction is ATP to ADP

A

Reversible - goes both way

109
Q

Which Enzymes help with ATP/ADP

A

ATPase: ATP –> ADP

ATP-synthase: ADP –> ATP

110
Q

3 Sources of ATP

A

1) Creatine Phosphate
2) Anaerobic Metabolism
3) Aerobic Metabolism

111
Q

What is Creatine Phosphate

A

Compound that is always present in our muscles

Generates ATP for max muscle contraction (short duration)

112
Q

Describe Anaerobic Metabolism in regards to ATP

A

Kicks in after CP
No O2 needed; uses Glucose from cellular respiration (steps 1 and 2)
Helps extend duration of max muscle contraction

113
Q

Describe Aerobic Metabolism in regards to ATP

A

Extends max muscle contraction duration from 40 secs-hours
Requires O2 and Glucose from cellular respiration (steps 3 and 4)
Taps into lipid sources