Unit 2 (Chemistry) Chapter 3 (Macromolecules) Flashcards

1
Q

Carbon

A

Basis of almost all molecules important for life

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2
Q

Organic Compounds

A

Carbon based molecules
- Usually contains hydrogen atoms
- Double bonds change the shape of a molecule

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3
Q

Carbon Skeleton

A

Chain of carbon atoms that makes the backbone of an organic molecule

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4
Q

Isomers

A

Compounds with the same chemical formula but different structures

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5
Q

Isomers in Pharmacology

A

2 Isomers of a drug may not be equally effective or have very different effects

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6
Q

Hydrocarbons

A

Molecules that consists of only hydrogen & carbon
- Major components of petroleum
- Found in areas with much larger complex compounds

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7
Q

Chemical Group

A

Atoms attached to the carbon skeleton

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8
Q

6 Chemical Groups

A
  1. Hydroxyl
  2. Carbonyl
  3. Carboxyl
  4. Amino group
  5. Phosphate group
  6. Methyl group
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9
Q

Polar Groups

A

Are hydrophilic
- Hydroxyl
- Carbonyl
- Carboxyl
- Amino
- Phosphate

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10
Q

Non-polar Groups

A

Are hydrophobic
- Methyl

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11
Q

Hydroxyl Group

A

Are alcohols

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12
Q

Carbonyl Group

A

Found in simple sugars

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13
Q

Carboxyl Group

A

Donates an H+ to a solution making it acidic

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14
Q

Amino Group

A

Getting an H+ from a solution and are called amines

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15
Q

Phosphate Group

A

Often ionized b/c O atoms are negative

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16
Q

Methyl Group

A

Affects gene expression

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17
Q

4 Classes of Macromolecules

A
  1. Carbohydrates
  2. Lipids
  3. Proteins
  4. Nucleic Acids
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18
Q

Macromolecules

A

Large molecules made of large polymers

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19
Q

Polymers

A

Small molecules joint together in chains
- Macromolecules are made of large polymers

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20
Q

Monomers

A

Building block of polymers

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21
Q

Dehydration Reaction

A

Removes a molecule of water as 2 molecules become bonded together
- OH- from 1 molecule, H+ from the other

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22
Q

How is a polymer made?

A

It is made through a dehydration reaction

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23
Q

Hydrolysis

A

Digestion of polymers into monomers
- Opposite of dehydration reaction
- OH- attaches to 1 monomer H+ attaches to the other

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24
Q

How are polymers broken?

A

It is broken through hydrolysis

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25
Carbohydrates
They are sugars or saccharides that can be small or large molecules which are mostly hydrophilic
26
Monosaccharides and an example
Simplest of sugars and are the main fuel for cells that contains a carbonyl & multiple hydroxyl groups. - Ex. Honey is made up of glucose & fructose (both are isomers)
27
How do Monosaccharides Form Rings
It creates rings with 3-7 carbons - Most are pentoses (5 carbons) & hexoses (6 carbons) - Pentoses & hexoses are the primary ring structures
28
Chemical Formula Characteristic of Monosaccharides
It is generally a multiple of CH2O
29
Disaccharides
Two monosaccharides linked together - Ex. Maltose = two glucose molecules
30
Polysaccharides
Hundreds or thousands of monosaccharides linked together that stores molecules & structural compounds
31
Four types of Polysaccharides
1. Starch 2. Glycogen 3. Cellulose 4. Chitin
32
Starch
It acts as a storage polysaccharide in plants - Coiled into a helical shape - Most animals have enzymes to hydrolyze starch - Main sources are potatoes & grains
33
Glycogen
The stored form of glucose in animals mostly in liver & muscle cells - Highly branched - Liver & muscle cells hydrolyze glycogen to release glucose molecules
34
Cellulose
Polymer of glucose - Cable-like microfibrils - Most abundant organic compound - Animals can't break it down - Some microorganisms can hydrolyze cellulose
35
Lipids
Fatty compounds that perform different functions on the body - All are hydrophobic - Smallest of the macromolecules - Not polymers made up of monomers
36
3 Types of Lipids
1. Fats 2. Phospholipids 3. Steroids
37
Fat
3 fatty acids linked to a glycerol molecule that stores energy - Synonym is triglyceride
38
Fat characteristics
- Gram of fat stores twice as much energy as a gram of carbohydrates - Plants store most their energy as carbohydrates - Animals store energy as fats
39
Glycerol
Small sugar
40
Fatty acids
Carboxyl group bound to a hydrocarbon chain - Hydrocarbon chains are non-polar
41
Unsaturated fatty acid
Hydrocarbon chain that has 1 or more bonds
42
Saturated fatty acid
Hydrocarbon chain that has single bonds - Will have the max possible number of hydrogen atoms
43
Characteristics of Unsaturated fatty acids
- Fats of most plants & fish - Kinks in fatty acid chains - Liquid at room temp
44
Characteristics of Saturated fatty acids
- Most animals fats - No bends in fatty acid chains - Solid at room temp
45
Partially Hydrogenated Oils
Unsaturated fats converted to saturated fats
46
Phospholipids
Major part of cell membranes - Similar structure to fats - Arranges as a double layered sheet with fatty acid tails in middle and glycerol heads on the outside
47
Steroids
Carbon skeleton of 4 fused rings - Different steroids vary in chemical groups attached to them - Ex. Cholesterol
48
Proteins
Polymer of small building blocks named amino acids - Almost all functions of body needs needs protein - Structurally and functionally most varied
49
Role of Proteins List
(ETDSRCSS) - Enzymes - Transport molecules - Defense proteins - Signaling proteins - Receptor proteins - Contractile proteins - Structural proteins - Storage proteins
50
Characteristics of Proteins
- Function of protein depends on structure - Each protein has a unique shape - Proteins must recognize and bind to other molecules to function
50
Globular Proteins
Most enzymes & many other proteins
51
Fibrous Proteins
Shape of protein makes the filament strong - Ex. Structural proteins in hair
52
Denaturation
Process where a protein unravels & loses its shape, therefore also losing function - Proteins fold spontaneously into correct shape - Ex. Heat can denature a protein
53
Effect of Incorrectly Folded Proteins
Can often cause diseases - Ex. Alzheimer's
54
Prions
Infectious misshapen proteins connected to degenerative brain disease - Ex. Mad cow disease
55
Amino Acids
Building blocks of proteins
56
Characteristics of Amino Acids
- 20 standard amino acids - All have an amino, carboxyl, and a variable chemical group (R group) - Hydrophobic amino acids have non-polar R groups - Hydrophilic amino acids have polar R groups
57
Peptide Bond
Dehydration reaction between a carboxyl group of one amino acid and the amino group of the other.
58
Dipeptide
Molecule (or peptide) made of 2 amino acids
59
Polypeptide
Chain of amino acids - Most proteins are at least 100 amino acids longs
60
Characteristics of Polypeptides
- Proteins are made of polypeptides - They must be coiled & folded into its final shape to make a protein - R groups on the amino acid affect the folding of polypeptides
61
Primary Structure
Sequence of amino acids in a polypeptide chain
62
Secondary Structure
Parts of the polypeptide chain coil & folds into regional patterns
63
Tertiary Structure
The overall 3D shape of the folded polypeptide
64
Quaternary Structure
Some protein consists of more than 1 polypeptide chain called subunits
65
Function of subunits
- Subunits interact with each other to complete the protein
66
Nucleic Acids
The 4th macromolecule
67
Gene
Unit of inheritance that determines the amino acid sequence of a polypeptide
68
DNA (deoxyribonucleic acid)
The nucleic acid that a gene is made of.
69
RNA (ribonucleic acid)
Nucleic acid that forms the polypeptide with instructions from DNA
70
Nucleotides
Monomers that make up nucleic acids - 5-carbon sugar - Phosphate group
71
Nitrogenous Base
Structure that contains nitrogen & carbon
72
Nitrogenous bases in DNA
- Adenine (A) - Thymine (T) - Guanine (G) - Cytosine (C)
73
Nitrogenous bases in RNA
- Adenine (A) - Thymine (T) - Cytosine (C) - Uracil (U)
74
Polynucleotide
Polymer built from nucleotide monomers - Nucleotides are bound together with a dehydration reaction - Sugar-phosphate backbone with nitrogenous bases outside of the backbone
75
Nucleic Acid Structure
- RNA: 1 polynucleotide strand - DNA: 2 polynucleotide strands wound into a double helix - A pairs T & G pairs C
76
Inheritance
DNA is the genetic material we inherit from our parents - DNA provides directions for its own replication
77
Gene Expression
Production of proteins using the instructions found in DNA