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Anatomy and Physiology > Macromolecules > Flashcards

Macromolecules Flashcards

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1
Q

Monomer

A

a monomer is a molecule with low molecular weight that can combine with others of the same kind to form a chemical compound known as a polymer.

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2
Q

Polymer

A

polymers are formed from multiple monomers connected together.

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3
Q

Dehydration synthesis

A

the creation of larger molecules from smaller monomers where a water molecule is released.

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4
Q

Hydrolysis Reaction

A

In a hydrolysis reaction, a larger molecule forms two (or more) smaller molecules and water is consumed as a reactant.
-involves adding water to one large molecule to break it into multiple smaller molecules

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5
Q

Carbohydrates

A
  • sugar and starches
  • C, H, O
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6
Q

Monosacharrides

A

Simple sugars containing three to seven carbon atoms

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7
Q

Disaccharides

A

Double sugars

  • Formed by dehydration synthesis of two monosaccharides

Too large to pass through cell membranes

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8
Q

Polysaccharides

A

Polymers of monosaccharides

Formed by dehydration synthesis of many monomers

Not very soluble

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9
Q

Formula of Monosaccharides

A

(CH2O)n: general formula

n = number of carbon atoms

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10
Q

Example of Monosaccharides

A

Pentose sugars

-Ribose and deoxyribose

Hexose sugars

-Glucose (blood sugar)

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11
Q

Example of Disaccharides

A

Sucrose, maltose, lactose

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12
Q

Lipids

A
  • Contain C, H, O, but less in carbohydrates, and sometimes contain P
  • Insoluble in water
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13
Q

Triglycerides

A

polymer of lipid

Called fat when solid oils when liquid

Made of saturated fatty acids (saturated in H atoms)

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14
Q

What are triglycerides made of?

A

Composed of three fatty acids (linear hydrocarbons) bonded to a glycerol molecule (sugar alcohol) by dehydration synthesis

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15
Q

Function of Triglycerides

A
  • Energy storage
  • Insulation
  • Protection
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16
Q

Saturated fatty acids

A

What Triglycerides are made of

A saturated fat is a type of fat in which the fatty acid chains have all single covalent bonds.

It is saturated with H atoms.

These create linear molecules which can pack closely together forming a solid at room temperature (Example: animal fats, butter)

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17
Q

Unsaturated fatty acids

A

Unsaturated fatty acid carbon chains contain one or more double bonds with a terminal carboxylic group (–COOH)

have less h atoms

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18
Q

Example of unsaturated fats

A

Trans fats – modified unsaturated fatty oils that resemble structure of saturated fats that are considered unhealthy

Omega-3 fatty acids – “heart healthy”

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19
Q

Phospholipids

A

Modified triglycerides

Important in cell membrane structure

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20
Q

What are phospholipids made of?

A

Glycerol and two fatty acids plus a phosphorus-containing group

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21
Q

Phospholipids structure

A

“Head” and “tail” regions have different properties

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22
Q

Head

A

Head is polar *charged and hydrophilic (attracted to water)

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23
Q

Tails

A

Tails are nonpolar and hydrophobic (repelled by water)

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24
Q

Steroid

A

Consist of four interlocking ring structures

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25
What is the function of steroids?
Starting material for synthesis of vitamin D, steroid hormones, and bile salts Important in cell plasma membrane structure
26
Steroids Example
Most important steroid is cholesterol
27
Steriods are made by
Made by liver and also found in animal products (ex: cheese, eggs, meat)
28
Eicosanoids
Derived from a fatty acid (arachidonic acid) found in cell membranes
29
Eicosanoids role
Play a role in blood clotting, control of blood pressure, inflammation, and labor contractions Inflammatory actions are blocked by NSAIDs (Ex: aspirin or ibuprofen)
30
Proteins functions
Have most varied functions of any molecules Structural - collagen chemical (enzymes) contraction (muscles)- actin and myosin Transport proteins Can act as either an acid or base
31
Peptide bonds
Polymers of amino acid monomers held together by peptide bonds
32
Proteins
- Contain C, H, O, N, and sometimes S and P -Comprise 20–30% of cell mass -
33
What are proteins made from?
All proteins are made from 20 types of amino acids Contain both an amine group and acid group
34
How do proteins differ?
Differ by which of 20 different “R groups” is present
35
What determines the shape and function of protein
Four levels of protein structure determine shape and function
36
What are four levels?
Primary, Secondary, Tertiary, and Quaternary
37
Primary
linear sequence of amino acids (order)
38
Secondary
how primary amino acids interact with each other
39
Types of Secondary Structure
Alpha (α) helix coils resemble a spring Beta (β) pleated sheets resemble accordion ribbons
40
Tertiary
how secondary structures interact
41
Quaternary
how 2 or more different polypeptides interact with each other
42
Shapes of Proteins
Fibrous or Globular
43
Fibrous
- Strandlike, water-insoluble, and stable - most have tertiary or quaternary structure
44
What do fibrous proteins do?
Provide mechanical support and tensile strength
45
Examples of fibrous proteins
keratin, elastin, collagen (single most abundant protein in body), and certain contractile fibers
46
Globular
Compact, spherical, water-soluble, and sensitive to environmental changes -Tertiary or quaternary structure (3-D)
47
What are active sites in globular proteins?
Specific functional regions (active sites)
48
Examples of globular proteins?
antibodies, hormones, molecular chaperones, and enzymes
49
Denaturation
globular proteins unfold and lose their functional 3-D shape Fibrous are more stable
50
Why do proteins denature?
Can be caused by decreased pH (increased acidity) or increased temperature Usually reversible if normal conditions restored Irreversible if changes are extreme
51
Enzyme
globular proteins that act as biological catalysts
52
Catalysts
regulate and increase speed of chemical reactions without getting used up in the process
53
Enzyme Function
Lower the energy needed to initiate a chemical reaction
54
Three Steps of Enzyme Process
1.Substrate binds to enzyme’s active site, temporarily forming enzyme-substrate complex 2.Complex undergoes rearrangement of substrate, resulting in final product 3. Product is released from enzyme
55
Nucleic Acid
Nucleic acids, composed of C, H, O, N, and P, are the largest molecules in the body
56
Monomer of Nucleic Acid
Nucleotides
57
What are nucleic acids made of?
Composed of nitrogen base, a pentose sugar, and a pHospHate group
58
Two major classes of nucleic acids
Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA)
59
DNA
holds the genetic blueprint for the synthesis of all proteins
60
Shape and Location of DNA
Double-stranded helical molecule (double helix) located in cell nucleus
61
Four Nitrogen Bases
Purines and Pyrimidines
62
Purines
adenine (A), guanine (G)
63
Pyrimidines
cytosine (C) and thymine (T)
64
Complementary Base Pairing Rules
A always pairs with T G always pairs with C
65
RNA
a single-stranded molecule which has a shorter chain of nucleotides and functions outside the nucleus - links DNA to protein synthesis
66
RNA Components
ribose sugars attached to nitrogenous bases and phosphate groups.
67
Uracil
This replaces Thymine in RNA A always pairs with U G always pairs with C
68
What are three varieties of RNA for protein synthesis?
Messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA)
69
ATP
Adenine-containing RNA nucleotide with two additional phosphate groups
70
ATP Function
Offers immediate, usable energy needed by body cells
71
How is energy released in ATP?
Chemical energy released when glucose is broken down is captured in ATP (adenosine triphosphate)
72
How does ATP help other molecules (related to work and energy)
Terminal phosphate group of ATP can be transferred to other compounds that can use energy stored in phosphate bond to do work
73
Loss of one phosphate results in
ATP to ADP
74
Loss of second phosphate results in
ADP to AMP
75
Order of Energy *highest to lowest
ATP ADP AMP
76
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Anatomy and Physiology (25 decks)

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