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CHAPTER 2
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The Chemical Elements
2-2
Element = simplest form of matter with
unique chemical properties
24 elements have biological role
6 elements = 98.5% of body weight
trace elements in minute amounts
Atomic number = # of protons in nucleus
periodic table
elements arranged by atomic number
2-3
Atomic Mass
Number of protons and neutrons in nucleus
Atomic mass units (amu)
Number of neutrons determined by subtracting the atomic
number from the mass number
2-4
Atomic Structure
2-5
Nucleus = center of atom
protons: single + charge, mass = 1 amu
neutrons: no charge, mass = 1 amu
Electron shells surround the nucleus
electrons: single negative charge, little mass
electrons swarm about the nucleus in electron shells
(energy levels)
valence electrons in the outermost shell
interact with other atoms
determine chemical behavior
Planetary Models
of
Elements
2-6
p+ represents protons, no represents neutrons
Electron Energy Levels
2-7
Each energy level can hold certain maximum
number of electrons
Maximum number determined by formula
X=2(n squared)
Isotopes and2-8Radioactivity
Isotopes
differ in # of neutrons
extra neutrons increase atomic weight
isotopes of an element are chemically similar
have same valence electrons
Atomic weight
average atomic mass of the isotopes
Radioisotopes and
Radioactivity
2-9
Isotopes
same chemical behavior, differ in physical behavior
breakdown gives off radiation
Radioisotopes
unstable isotopes
every element has at least one radioisotope
Radioactivity
radioisotopes decay to stable isotopes releasing
radiation
we are all mildly radioactive
Ions and Ionization
2-10
• Ions - carry a charge due to an unequal
number of protons and electrons
Ionization =
transfer of
electrons from
one atom to
another
( stability of
valence shell)
Anions and Cations
• Anion
2-11
– atom that gained electrons (net negative charge)
• Cation
– atom that lost an electron (net positive charge)
• Ions with opposite charges are attracted to each
other
Electrolytes
2-12
Salts that ionize in water to form body fluids
Form solutions capable of conducting electricity
Electrolyte importance
chemical reactivity
osmotic effects (influence water movement)
electrical effects on nerve and muscle tissue
Imbalances cause muscle cramps, brittle
bones, coma and death
2-13
Free Radicals
2-14
Particle with an odd number of electrons
Produced by
normal metabolic reactions, radiation, chemicals
Causes tissue damage
reactions that destroy molecules
causes cancer, death of heart tissue and aging
Antioxidants
neutralize free radicals
in diet (vitamin E, carotenoids, vitamin C)
Molecules and 2-15
Chemical Bonds
Molecules
two or more atoms covalently bonded
Compounds
two or more atoms of different elements covalently
bonded
Molecular formula
elements and how many atoms of each
Structural formula
location of each atom
structural isomers revealed
Structural Formula of Isomers
2-16
Molecular formulae are identical, but structural
formulas differ for grain alcohol and ether
Molecular
2-17 Weight
MW of compound = sum of atomic weights
of atoms
Calculate: MW of glucose (C6H12O6)
6 C atoms x 12 amu each = 72 amu
12 H atoms x 1 amu each = 12 amu
6 O atoms x 16 amu each = 96 amu
Molecular weight (MW) = 180 amu
Chemical
2-18 Bonds
Ionic bonds
Covalent bonds
Hydrogen bonds
Van der Waals force
Chemical Bonds Song
2-19
http://www.youtube.com/watch?v=BCYrNU-
7SfA&feature=related
Ionic Bonds
2-20
Attraction of oppositely charged ions
No sharing of electrons
Weak bond (easily dissociates in water)
Covalent
2-21 Bonds
Formed by sharing of valence electrons
Types of covalent bonds
single = sharing of single pair electrons
double = sharing of 2 pairs
nonpolar
shared electrons (equal time around each nucleus)
strongest of all bonds
polar
negative charge where electrons spend most time
Single Covalent Bond
2-22
One pair of electrons are shared
Double covalent bonds:
Two pairs of electrons are shared each C=O bond
2-23
Nonpolar /Polar Covalent Bonds
2-24
electrons shared
equally
electrons
shared
unequally
Hydrogen Bonds
2-25
Weakest bond = no sharing of electrons
Attraction between polar molecules
positive hydrogen atoms to negative oxygen atoms
in a 2nd molecule
Physiological importance
properties of water created by shapes of large
complex molecules
determined by folding due to hydrogen bonds
Hydrogen Bonding in Water
2-26
Water animation
2-27
http://www.youtube.com/watch?v=KiZJOTt3Dl0&f
eature=related
Van der Waals Forces
2-28
Weak attractions between neutral atoms
Fluctuations in electron density create
polarity
Only 1% as strong as a covalent bond
folding of large molecules
significant when 2 large surfaces meet
Mixtures and Water
2-29
Substances physically but not chemically combined
Mixtures in our body contain water
Water 50-75% of body weight
Depends on age, sex, percentage body fat, etc
Solvency= ability to dissolve other chemicals
2-30
Hydrophilic (charged substances) dissolve easily in
water
Hydrophobic (neutral substances) do not easily
dissolve in water
Water= universal solvent
Metabolic reactions and transport of substances
Water as a Solvent
2-31
Polar water molecules overpower the ionic bond in Na+Cl-forming hydration spheres around each ion
-water molecules: negative pole faces Na+, positive pole
faces Cl-
Adhesion and Cohesion
2-32
Adhesion- tendency of one substance to cling to
another
Cohesion-tendency of like molecules to cling to each
other
water is very cohesive due to its hydrogen bonds
surface film on water formed by surface tension
Chemical Reactivity of Water
2-33
Participation in chemical reactions
Water ionizes into H+ OH Water ionizes other chemicals (acids and salts)
Water involved in hydrolysis and dehydration synthesis
reactions
Thermal Stability of Water
2-34
Water stabilizes internal temperature
Has high heat capacity
Hydrogen bonds inhibit temperature increases by inhibiting
molecular motion
Water absorbs heat without changing temperatures
Effective coolant
1 ml of perspiration removes 500 calories
Calorie: amount of heat required to raise temperature of 1 g of water
by 1 degree C
Solutions
2-35
Mixture of a solute
into a solvent
Small solute particles
Pass through cell membranes
Solution transparent
Remains mixed
Colloids
2-36
Mixture of protein and water
Change from liquid to gel state within
and between cells
Particles too large to pass
through cell membranes
Cloudy
Remains mixed
Suspensions and Emulsions
2-37
Suspension
Particles suspended in a solvent
Particles exceed 100nm
Too large to pass through cell
membrane
Cloudy or opaque appearance
Separates on standing
Emulsion
-suspension of one liquid in
another
-fat in breast milk
Measures of Concentration
2-38
Weight per Volume
weight of solute in given volume of solution
IV saline: 8.5 grams NaCl/liter of solution
Percentages
Weight/volume of solute in solution
IV D5W (5% w/v dextrose in distilled water)
5
grams of dextrose and fill to 100 ml
water
Molarity
moles of solute/liter in solution
physiologic effects based on number of
molecules in solution not on weight
Molarity
2-39
Molecular weight in grams = 1 mole of
molecules
1 mole = Avogadro’s number of molecules
Molarity is the number of moles of solute/
liter of solution
MW of glucose is 180
one-molar (1.0M) glucose solution contains
180g/L
Percentage vs. Molar Concentrations
2-40
Percentage
# of molecules
unequal
weight of solute
equal
Molar
# of molecules equal
weight of solute
unequal
Electrolyte Concentrations
2-41
Effect the body chemically, physically and
electrically
depends on charge and concentration
Measured in equivalents
1 Eq will electrically neutralize 1 mole of H+ or
OH- ions
multiply molar concentration x valence of the ion
1 M Na+ = 1 Eq/L
1 M Ca2+ = 2 Eq/L
Acids, Bases and pH
2
4
2
An acid is proton donor (releases H+
ions)
A base is proton acceptor (accepts H+
ions)
pH = the concentration of H+ ions in
solution
a pH of less than 7 is acidic solution
a pH of greater than 7 is basic solution
a pH of 7.0 is neutral pH
pH= -log [H+]
Acids
Proton Donor
HX H+ + X-
Bases
Proton Acceptor
YOH Y+ + OH-
Strong acid
Strong acid– ionizes completely in an aqueous
solution
H2O + HCl H3O+ ClAlso sulphuric acid and nitric acid
Have pH around 0 to 1
The lower the pH the higher the conc of hydrogen
ions in the solution
Weak acid
Does not ionize completely when it is dissolved in
water
Ex. Ethanoic acid
CH3COOH + H2O > CH3cOO- + H3O
Most organic acids are weak
Strong Base
A base which hydrolyses completely, raising the pH
of the solution towards 14
Weak Base
A base that doesn’t convert fully into hydroxide ions
in solution
Ex. ammonia
pH Scale
2-48
Buffers
Maintains a constant pH upon the addition of small
amounts of either acid or base
2 parts to a buffer-weak acid and a weak base
Acid- can donate H+ ion if [H+] decreases
Base- can accept H+ ion if [H+] increases
Examples in body are bicarbonate buffer and
phosphate buffers
Salts
Mixing an acid and a base results in water and salt
A compound that yields ions other than hydrogen
ions is called a salt
Electrolytes
Acids, bases, and salts are called electrolytes
Solutions of electrolytes conduct electricity because
of the presence of ions
Would a solution of hydrochloric acid be an
electrolyte?
HCl H+ + Cl-
Work and Energy
2-52
Energy- capacity to do work
Kinetic energy- energy of motion
Heat is kinetic energy of molecular motion
Potential energy- energy due to object’s position
(ions on one side only of cell membrane)
Chemical energy-potential energy stored in the molecular
bonds
Chemical Reaction
2-53
Process that forms or breaks an ionic or
covalent bond
Symbolized by chemical equation
reactants products
Classes of reactions
Synthesis reactions
Decomposition reactions
Exchange reactions
Reversible reactions
Synthesis Reactions
2-54
Two or more small molecules
combine to form a larger one
A + B AB
Decomposition Reactions
2-55
Large molecules broken
down into smaller ones
AB A + B
Exchange Reactions
Two molecules collide and exchange atoms or
2-56
group of atoms
AB+CD ABCD
Stomach acid
(HCl) and sodium
bicarbonate
(NaHCO3) from the
pancreas combine
to form NaCl and
H2CO3.
AC + BD
Exchange Reactions
2-57
Single exchange
AB+C AC+B
Double exchange
AB+CD AD + CB
Reversible Reactions
2-58
Go in either direction (symbolized with
double-headed arrow)
A + B AB
CO2 + H2O <->
H2CO3 <->
carbonic acid
HCO3- + H+
bicarbonate
Law of mass action determines direction
side of equation with greater quantity of
reactants dominates
Reaction Rates
2-59
Basis for reactions is molecular motion and
collisions
reactions occur when molecules collide with
enough force and the correct orientation
Reaction Rates affected by:
concentration
temperature
more concentrated, more collisions, faster rate
higher temperature, greater collision force, faster rate
Catalysts (enzymes)
speed up reactions without permanent change to itself
holds reactant molecules in correct orientation
Metabolism
2-60
All the chemical reactions of the body
Catabolism
energy releasing (exergonic) decomposition
reactions
breaks covalent bonds, produces smaller molecules,
releases useful energy
Anabolism
energy storing (endergonic) synthesis reactions
requires energy input
Oxidation-Reduction Reactions
2-61
Oxidation
molecule gives up electrons and releases energy
accepting molecule is the oxidizing agent
oxygen is often the electron acceptor
Reduction
molecule gains electrons and energy
donating molecule is the reducing agent
Oxidation-reduction (redox) reactions
Electrons are often transferred as hydrogen atoms
2-62
Organic Chemistry
2-63
Study of compounds containing carbon
4 categories of carbon compounds
carbohydrates
lipids
proteins
nucleotides and nucleic acids
Organic Molecules and Carbon
2-64
Only 4 valence electrons
bonds readily to gain more valence electrons
Forms long chains, branched molecules and
rings
serve as the backbone for organic molecules
Carries a variety of functional groups
Functional Groups
2-65
Atoms attached to carbon
backbone
Determines chemical
properties
Monomers and Polymers
2-66
Macromolecules = very large molecules
Polymers = macromolecules formed from
monomers bonded together
Monomers = an identical or similar subunit
Polymerization
2-67
Bonding of monomers together to form a
polymer
Formed by dehydration synthesis
starch molecules are a polymer of 3000 glucose
monomers
protein molecules are a polymer of amino acids
Dehydration Synthesis
2-68
Monomers covalently bond together to
form a polymer with the removal of a water
molecule
A hydroxyl group is removed from one monomer
and a hydrogen from the next
Hydrolysis
2-69
Splitting a polymer (lysis) by the addition of a
water molecule (hydro)
a covalent bond is broken
All digestion reactions consists of hydrolysis
reactions
Organic Molecules: Carbohydrates
2-70
Hydrophilic organic molecule
General formula
(CH2O)n
n = number of carbon atoms
for glucose, n = 6, so formula is C6H12O6
2:1 ratio of hydrogen to oxygen
Names of carbohydrates
word root sacchar- or the suffix -ose often used
monosaccharide or glucose
Monosaccharides
2-71
Simple sugars
General formula is C6H12O6
structural isomers
• Major monosaccharides
– glucose, galactose and
fructose
– produced by digestion of
complex carbohydrates
• glucose is blood sugar
Disaccharides
2-72
Sugar molecule
composed of 2
monosaccharides
Major disaccharides
sucrose = table sugar
Lactose = sugar in milk
glucose + fructose
glucose + galactose
Maltose = grain
products
glucose + glucose
Polysaccharides
2-73
Chains of glucose subunits
Starch: energy storage in plants
digestible by humans for energy
Cellulose: structural molecule of plant cell walls
fiber in our diet
Glycogen: energy storage in animals
liver synthesizes after a meal and breaks down between
meals
Carbohydrate Functions
2-74
All digested carbohydrates converted to
glucose and oxidized to make ATP
Conjugated carbohydrate = bound to lipid or
protein
glycolipids
external surface of cell membrane
glycoproteins
external surface of cell membrane
mucus of respiratory and digestive tracts
proteoglycans
gels that hold cells and tissues together
joint lubrication
rubbery texture of cartilage
2-75
Organic Molecules: Lipids
2-76
Hydrophobic organic molecule
composed of carbon, hydrogen and oxygen
Less oxidized and thus has more calories/gram
Five primary types in humans
fatty acids
triglycerides
phospholipids
eicosanoids
steroids
Fatty Acids
2-77
Chain of 4 to 24 carbon atoms
carboxyl (acid) group on one end, methyl group on the
other and hydrogen bonded along the sides
Classified
saturated - carbon atoms saturated with hydrogen
unsaturated - contains C=C bonds without hydrogen
Triglycerides (Neutral Fats)
2-78
3 fatty acids bonded to glycerol molecule
(dehydration synthesis)
At room temperature
when liquid called oils
often polyunsaturated fats from plants
when solid called fat
saturated fats from animals
Function - energy storage, insulation and shock
absorption
Phospholipids
2-79
Triglyceride with one fatty acid replaced by a
phosphate group
Amphiphilic character
fatty acid “tails” are hydrophobic
Phosphate “head” is hydrophilic
Eicosanoids
2-80
Derived from arachidonic acid (a fatty acid)
Hormone-like chemical signals between cells
Includes prostaglandins – produced in all
tissues
role in inflammation, blood clotting, hormone
action, labor contractions, blood vessel diameter
Steroids and Cholesterol
2-81
Steroid = lipid with carbon atoms in four
rings
all steroids are derived from cholesterol
cortisol, progesterone, estrogens, testosterone and bile
acids
Cholesterol
important component of cell membranes
produced only in animal liver cells
naturally produced by our body
2-82
Organic Molecules: Proteins
2-83
• Protein = polymer of amino acids
• Combination determines structure and
function
• Amino acid = carbon with 3 attachments
– Amino (NH2), carboxy (COOH) and radical
group (R group)
• 20 unique amino acids
– -R groups differ
– properties determined by -R group
Naming of Peptides
2-84
Peptide = polymer of 2 or more amino acids
Named for the number of amino acids
dipeptides have 2, tripeptides have 3
oligopeptides have fewer than 10 to 15
polypeptides have more than 15
proteins have more than 100
Dipeptide Synthesis
2-85
•Dehydration synthesis creates a peptide bond that joins amino
acids
Protein Structure and Shape
2-86
Primary structure
amino acid sequence
Secondary structure
coiled or folded shape
hydrogen bonds between negative C=O and positive
N-H groups
Tertiary structure
further folding and bending into globular and
fibrous shapes
Quaternary structure
associations of two or more separate polypeptide
chains
2-87
Conjugated Proteins
2-88
Contain a non-amino acid moiety
Hemoglobin contains complex iron
containing ring called a heme moiety
Protein Conformation and
Denaturation
2-89
Conformation – unique 3-D shape crucial to
function
ability to reversibly change their conformation
opening and closing of cell membrane pores
Denaturation
conformational change that destroys function
extreme heat or pH
Protein Functions
2-90
Structure
collagen, keratin
Communication
some hormones, cell receptors
Membrane Transport
channels, carriers
Catalysis
enzymes
Protein Functions 2
2-91
Recognition and protection
antigens, antibodies and clotting proteins
Movement
molecular motor = molecules that can change shape
repeatedly
Cell adhesion
proteins bind cells together
Enzymes
2-92
Proteins as biological catalysts
promote rapid reaction rates
Substrate - substance an enzyme acts upon
Naming Convention
named for substrate with -ase as the suffix
amylase enzyme digests starch (amylose)
Lowers activation energy = energy needed to
get reaction started
enzymes facilitate molecular interaction
Enzymes and Activation Energy
2-93
Steps of an Enzyme Reaction
2-94
Substrate approaches enzyme molecule
Substrate binds to active site forming enzyme-
substrate complex
highly specific
Enzyme breaks bonds in substrate
Reaction products released
Enzyme repeats process over and over
Enzymatic Reaction Steps
2-95
Enzymatic Action
2-96
Reusability of enzymes
enzymes are unchanged by the reactions
Astonishing speed
millions of molecules per minute
Temperature and pH
change shape of enzyme and alter its ability to
bind
enzymes vary in optimum pH
salivary amylase works best at pH 7.0
pepsin works best at pH 2.0
temperature optimum for human enzymes =
body temperature
Cofactors and Coenzymes
2-97
Cofactors
nonprotein partners (iron, copper, zinc, magnesium or
calcium ions)
bind to enzyme and change its shape
essential to function
Coenzymes
organic cofactors derived from water-soluble vitamins
(niacin, riboflavin)
transfer electrons between enzymes
Coenzyme NAD+
2-98
NAD+ transports electrons from one metabolic
pathway to another
Metabolic Pathways
2-99
Chain of reactions, each catalyzed by an enzyme
ABCD
A is initial reactant, B+C are intermediates and
D is the end product
Regulation of metabolic pathways
activation or deactivation of the enzymes
cells can turn on or off pathways
Organic Molecules: Nucleotides
2100
3 components
nitrogenous base
sugar (monosaccharide)
one or more phosphate groups
Physiological important nucleotides
ATP = energy carrying molecule
cAMP = activates metabolic pathways
DNA = carries genetic code
RNA = assists with protein synthesis
ATP (Adenosine Triphosphate)
2101
ATP contains adenine, ribose and 3 phosphate groups
ATP
2102
Holds energy in covalent bonds
2nd and 3rd phosphate groups have high energy bonds ~
ATPases hydrolyze the 3rd high energy
phosphate bond
separates into ADP + Pi + energy
Phosphorylation
addition of free phosphate group to another molecule
Overview of ATP Production
2103
ATP consumed within 60 seconds
Continually replenished
Other Nucleotides
2104
Cyclic adenosine monophosphate (cAMP)
formed by removal of both high energy Pi’s from ATP
formation triggered by hormone binding to cell surface
cAMP becomes “second messenger” within cell
activates effects inside cell
Nucleic Acids
2105
DNA (deoxyribonucleic acid)
100 million to 1 billion nucleotides long
contains genetic code
cell division, sexual reproduction, protein synthesis
RNA (ribonucleic acid) – 3 types
transfer RNA, messenger RNA, ribosomal RNA
70 to 10,000 nucleotides long
involved in protein synthesis coded for by DNA