A & P Chapter 2

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1

Matter

anything that takes up space and has mass, made up of atoms

2

atoms

the smallest stable units of matter, join together to form chemicals with different characteristics

3

chemical characteristics

determine physiology on the molecular and cellular level

4

Subatomic Particles

Proton - Positive charge, 1 mass unit
Neutron - Neutral, 1 mass unit
Electron - Negative charge, low mass

5

Atomic Structure

Nucleus - Contains protons and neutrons
Electron cloud - contains electrons

6

Atomic number

number of protons

7

Mass number

number of protons plus neutrons

8

Atomic weight

exact mass of all particles (daltons)
1 Dalton (Da) = 1.66 x 10-24grams (g) = the mass of
one proton or neutron

9

Isotopes

2 or more elements with equal numbers of protons but different numbers of neutrons

10

Chemical Bonds

Involve the sharing, gaining, and losing of electrons in the valence shell

11

Three major types of chemical bonds

1. Ionic bonds 2. Covalent bonds 3. Hydrogen bonds

12

Ionic bonds

Attraction between cations (electron donor) and
anions (electron acceptor) are atoms with positive or negative charge

13

Covalent bonds

Formed between atoms that share electrons
Strong electron bonds involving shared electrons
Non polar covalent bonds: equal sharing of electrons
Polar covalent bonds: unequal sharing of electrons

14

Hydrogen bonds

Weak polar bonds based on partial electrical attractions

15

Free Radicals

Ion or molecule that contain unpaired electrons in the outermost shell.
Extremely Reactive
typically enter into destructive reactions
Damage/destroy vital compounds

16

Hydrogen Bonds

Attractive force between polar covalent molecules
•Weak force that holds molecules together
•Hydrogen bonds between H2O molecules cause surface tension

17

Molecules

Two or more atoms joined by strong bonds

18

Compounds

Two or more atoms OF DIFFERENT ELEMENTS joined by strong or weak bonds Compounds are all molecules, but not all molecules are compounds

19

Energy

the capacity to do work

20

Work

a change in mass or distance

21

Forms of Energy

1. Kinetic energy 2. Potential energy 3. Chemical energy

22

Kinetic energy

energy of motion

23

Potential energy:

stored energy

24

Chemical energy

potential energy stored in chemical bonds

25

When energy is exchanged, heat is produced

cells cannot capture it or use it for work

26

Chemical Reactions

•Decomposition Reaction (Catabolism)
– Breaks chemical bonds
– AB -> A + B
– Hydrolysis A-B+H2O -> A-H + HO-B
•Synthesis Reaction (Anabolism)
–Forms chemical bonds
–A + B->AB
–Dehydration synthesis (condensation reaction)
•Exchange Reaction
-AB + CD->AD + CB
-Involves decomposition first, then synthesis
•Reversible reaction
-AB + CD-><-AD + CB
-At equilibrium the amounts of chemicals do not
change even though the reactions are still occurring

27

Reaction’s Components

Reactants:

materials going
into
a reaction

Products:

materials coming
out
of a reaction

Enzymes:

proteins that lower the activation energy of a
reaction

28

Reactants

materials going into a reaction

29

Products

materials coming out of a reaction

30

Enzymes

proteins that lower the activation energy of a
reaction are protein catalysts that lower the activation energy of reactions most chemical reactions that sustain life cannot occur unless the right enzymes are present

31

Activation energy

the amount of energy needed to get a reaction started

32

Exergonic (Exothermic)reactions

produce more energy than they use heat will be the by product

33

Endergonic (Endothermic)reactions

use more energy than they produce

34

Organic molecules

molecules based mostly on carbon and hydrogen (Carbohydrates, proteins, lipids, and nucleic acids)

35

Inorganic molecules

molecules not based mostly on carbon and
hydrogen (Carbon dioxide, oxygen, water, and inorganic acids,bases, and salts)

36

Essential Molecules

1.nutrients 2. metabolites

37

Nutrients

essential molecules obtained from food

38

Metabolites

molecules made or broken down in the body

39

Why is water so important to life?

Water accounts for up to two-thirds of your total body weight

40

Properties of Water

1. Solubility 2. Reactivity 3. high heat capacity 4. Lubrication

41

Solubility

water’s ability to dissolve a solute in a solvent
to make a solution

42

Reactivity

most body chemistry uses or occurs in water

43

High heat capacity

water’s ability to absorb and retain heat

44

Lubrication

to moisten and reduce friction

45

Aqueous Solutions

Polar water molecules form hydration spheres
around ions and small polar molecules to keep them in solution

46

The Properties of Aqueous Solutions

Hydrophilic and hydrophobic compounds

47

Hydrophilic

hydro = water,
philos = loving
Interacts with water Includes ions and polar molecules

48

Hydrophobic

phobos = fear
Does NOT interact with water
Includes non polar molecules, fats, and oils
Electrolytes and body fluids

49

Electrolytes

are inorganic ions that conduct electricity in solution Electrolyte imbalance seriously disturbs vital body functions

50

Colloid

A solution of very large organic molecules
For example, blood plasma

51

Suspension

A solution in which particles settle (sediment)
For example, whole blood

52

Concentration

The amount of solute in a solvent (mol/L, g/L)

53

pH

The concentration of hydrogen ions (H+) in a
solution

54

Hydrogen Ions: H+

Unbound protons
•Have important biological effects
•Form when water ionizes:
H2O -> H+ + OH-
Hydrogen Ion (or Proton) Water Hydroxide Ion

55

Neutral pH

a balance of H+ and OH—
–pure water = 7.0

56

Acid (acidic)

pH lower than 7.0
– high H+ concentration
- low OH— concentration

57

Base (basic)

pH higher than 7.0
– low H+ concentration
- high OH— concentration

58

pH Scale

card image

Has an inverse relationship with H+ concentration:
–more H+ ions mean lower pH, less H+ ions mean
higher pH

59

Acidosis

Excess H+ ions (low pH
–damages cells and tissues
–alters proteins
–interferes with normal physiological functions

60

Alkalosis

Excess OH— ions (high pH)
–Uncontrollable and sustained skeletal muscle contraction

61

Controlling pH

salts and buffers

62

Salts

–positive or negative ions in solution
–contain no H+ or OH
—(NaCl)

63

Buffers

–weak acid/salt compounds
–neutralizes either strong acid or strong base
Minimizes extreme shifts in pH
•Partnership between weak acids and bases, which work as pair to counter shifts in pH
•Example: Carbonic Acid
-Bicarbonate Buffer System
–When blood pH rises, carbonic acid dissociates to form bicarbonate and H+H2C03----> HC03-+ H+–
When blood pH drops, bicarbonate binds H+ to form carbonic acid HC03-+ H+-----> H2C03

64

Organic Molecules

-Contain H, C, and usually O
-Are covalently bonded
-Contain functional groups that determine chemistry: Carbohydrates Lipids Proteins (or amino acids) Nucleic acids

65

Carbohydrates

Contain carbon, hydrogen, and oxygen in a 1:2:1
ratio

66

Monosaccharides

Simple sugars with 3 to 7 carbon atoms
Glucose, fructose, galactose

67

Disaccharides

Two simple sugars condensed by dehydration synthesis Sucrose, maltose

68

Polysaccharides

Many monosaccharides condensed by dehydration synthesis Glycogen, starch, cellulose

69

Simple Sugars

Structural Formula:
•Straight
-chain form
•Ring from
•3-D
Isomers: Glucose vs. Fructose:
-Same chemical formula but different shape

70

Glycogen

made and stored in muscle cells

71

Lipids

-Mainly hydrophobic molecules such as fats, oils,
and waxes
-Made mostly of carbon and hydrogen atoms (1:2),
and some oxygen

72

Type of lipids

Fatty acids
Eicosanoids
Glycerides
Steroids
Phospholipids and glycolipids

73

Fatty Acids

-Long chains of carbon and hydrogen with a
carboxyl group (COOH) at one end
-Are relatively nonpolar, except the carboxyl group
-Fatty acids may be:
Saturated with hydrogen (single covalent bonds)
Unsaturated (one or more double bonds)
Lauric acid demonstrates two structural characteristics common to all fatty acids:
a long chain of carbon atoms and a carboxyl
group (—COOH) at one end

74

Monounsaturated

one double bond

75

Polyunsaturated

two or more double bonds

76

Eicosanoids

derived from the fatty acid called arachidonic acid
Used for cellular communication Never burned for energy

77

Leukotrienes

Active in immune system Used by cells to signal injury

78

Prostaglandins

Local hormones, short
-chain fatty acids Used for cell-to-cell signaling to coordinate events

79

Glycerides

Fatty acids attached to a glycerol molecule Triglycerides are the three fatty
-acid tails Also called triacylglycerols or neutral fats

80

Glycerides have three important functions

1.Energy source 2.Insulation 3.Protection

81

Steroids

Four rings of carbon and hydrogen with an assortment of functional groups

82

Types of steroids

1.Cholesterol 2.Estrogens and testosterone
3.Corticosteroids and calcitriol 4.Bile salts

83

Cholesterol

Component of plasma (cell) membranes

84

Estrogens and testosterone

Sex hormones

85

Corticosteroids and calcitriol

Tissue metabolism and mineral balance

86

Bile salts

Derived from steroids Processing of dietary fats

87

Diglycerides

attached to either a phosphate group (phospholipid) or a sugar (glycolipid)
Generally, both have hydrophilic heads and
hydrophobic tails and are structural lipids,
components of plasma (cell) membranes

88

Proteins

Are the most abundant and important organic molecules Contain basic elements
-Carbon (C), hydrogen (H), oxygen (O), and nitrogen (N)
-Basic building blocks
-20 amino acids

89

Seven Major Protein Functions

1.Support •Structural proteins
2.Movement •Contractile proteins
3.Transport •Transport (carrier) proteins
4.Buffering •Regulation of pH
5.Metabolic Regulation •Enzymes
6.Coordination and Control •Hormones
7.Defense •Antibodies

90

Protein Structure

Long chains of amino acids
structure of an Amino Acid
Five components of amino acid structure

91

Shape and Function

Protein function is based on shape
•Shape is based on sequence of amino acids

92

Denaturation

loss of shape and function due to heat or pH

93

Protein Shape

1.Primary structure 2.Secondary structure 3.Tertiary structure 4.Quaternary structure

94

Primary structure

The sequence of amino acids along a
polypeptide

95

Secondary structure

Hydrogen bonds form spirals or pleats

96

Tertiary structure

Secondary structure folds into a unique shape

97

Quaternary structure

Final protein shape — several tertiary
structures together

98

Enzymes

-Catalysts
-Proteins that lower the activation energy of a chemical reaction
-Not changed or used up in the reaction

99

Enzymes also exhibit

1.Specificity—will only work on limited types of
substrates
2.Saturation Limits—by their concentration
3.Regulation—by other cellular chemicals

100

Enzyme Function

Cofactor, Coenzyme, Isozymes

101

Cofactor

An ion or molecule that binds to an enzyme before
substrates can bind

102

Coenzyme

Nonprotein organic cofactors (vitamins)

103

Isozymes

Two enzymes that can catalyze the same reaction

104

Glycoproteins

Large protein + small carbohydrate Includes enzymes, antibodies, hormones, and mucus
production

105

Proteoglycans

Large polysaccharides + polypeptides Promote viscosity

106

Nucleic Acids

Nucleic Acids (C, H, O, N, and P) Are large organic molecules, found in the nucleus, which
store and process information at the molecular
level

107

Deoxyribonucleic acid (DNA)

Determines inherited characteristics Directs protein synthesis Controls enzyme production
Controls metabolism

108

Ribonucleic acid (RNA)

Controls intermediate steps in protein synthesis

109

DNA Polymerase

Enzyme that catalyzes the covalent bond between the phosphate of one nucleotide and the deoxyribose (sugar) of the next nucleotide

110

DNA Replication

3’ end has a free deoxyribose
5’ end has a free phosphate
DNA polymerase:
•can only build the new strand in the 5’ to 3’ direction
•Thus scans the template strand in 3’ to 5’ direction

111

Types of RNA

-Messenger RNA (mRNA)
-Transfer RNA (tRNA)
-Ribosomal RNA (rRNA)

112

Nucleotides Can Be Used to Store Energy

Adenosine diphosphate (ADP)
Two phosphate groups; di-= 2
Adenosine triphosphate (ATP)
Three phosphate groups; tri-= 3

113

Phosphorylation

Adding a phosphate group to ADP with a high
-energy bond to form the high
-energy compound ATP

114

Adenosine triphosphatase (ATPase)

The enzyme that catalyzes the conversion of ATP to
ADP

115

High-Energy Compounds:
ADP and ATP

-Assembled using Nucleotides
-Bonds are broken by cells to release energy as
needed
-During digestion and cellular respiration:
-energy from food is transferred to high energy
compounds for quick and easy access.