Chemical composition of the human body

Carbon (C): 18.5%

Oxygen (O):
65.0%
Calcium (Ca): 1.5%
Phosphorus (P): 1.0%
Potassium (K): 0.4%
Sulfur (S): 0.3%
Sodium (Na): 0.2%
Chlorine (Cl): 0.2%
Magnesium (Mg): 0.1%
Hydrogen (H):
9.5%
Trace elements: less than 0.01%
Boron (B) Manganese (Mn)
Chromium (Cr) Molybdenum (Mo)
Nitrogen (N):
Cobalt (Co) Selenium (Se)
3.3%
Copper (Cu) Silicon (Si)
Fluorine (F) Tin (Sn)
Iodine (I) Vanadium (V)
Iron (Fe) Zinc (Zn)
3-2
 Atoms
2 + Protons
Nucleus
2 Neutrons
Nucleus
2  Electrons

Electron cloud
+ containing two
+ electrons


Covalent Bonds
 Ionic Bonds

Na Cl Na+ Cl

Na Cl Na+ Cl
Sodium atom Chlorine atom
Sodium ion Chloride ion

Sodium chloride (NaCl)

Hydrogen Bonds

( )
Hydrogen bond
(+)

H Slightly positive
charge
( ) O
(+) H Slightly negative
(+) charge
( ) ( )

(+)
 Molecules
Electron Structural Space-filling Ball-and-stick
configuration formula model model

O
O
Double
bond C
C
Single H H
H H bond

Name (molecular formula) : Formaldehyde (CH2O)

Chemical Reactions
Chemical Reactions
 Structure/Function: Water
 The polarity of water molecules and the hydrogen bonding
that results explain most of water’s life-supporting
properties.

The abundance of water is a major reason that Earth is

habitable. Your cells are composed of 70–95% water.
Water’s four emerging properties that
contribute to the fitness of life on Earth:

1. the cohesive nature of water,

2. the ability of water to moderate
temperature,
3. Expansion upon freezing, and
4. the versatility of water as a solvent.
 Cohesion and water
Evaporation from the leaves transport in plants

Microscopic water-
conducting tubes
Cohesion due to
hydrogen bonds
between water
molecules
Colorized
SEM
Water Moderates Temperature
Water expands upon freezing
 Water: A versatile solvent
Sodium ion
Chloride ion in solution
in solution
Cl Na+

Na+
Cl

Salt crystal
 Chapter 3

 Carbohydrates
 Proteins
 Nucleic acids
 Lipids

3-17
 Organic Chemistry

 All organic molecules contain carbon.

– Inorganic molecules do not contain carbon.
 Biochemistry is the chemistry of living things.

3-18 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Carbon: The Central Atom

 Carbon is the central

atom in all organic
molecules.
 Carbon has unique
bonding properties.
– Can combine with other
carbon atoms in long
chains
– Can form ring structures

3-19 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Carbon: The Central Atom

 Carbon atoms
participate in four
covalent bonds.
– Has four electrons in the
outer energy level
– Can double bond with
oxygen
– Can triple bond with
other carbon atoms

3-20 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Properties of an Organic
Molecule

 Several factors determine the properties of an

organic molecule.
– The types of atoms in the molecule
– The 3-D arrangement of atoms within the molecule

3-21 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Isomers

Organic molecules can have the same

number and composition of atoms, but can
have different arrangements.

These are called isomers.

Molecules with the same empirical formula but
different structural formulas

3-22 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Hexose Isomers
 Hexose Isomers

3-24 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 The Carbon Skeleton

 All organic molecules have a carbon skeleton.

– This determines the overall shape of the molecule.
 Organic molecules differ in these ways:
– The length and arrangement of the carbon skeleton
– The kinds and location of atoms attached to it
– How the attached atoms are combined together
 These combinations are called functional groups.
 Functional groups determine the chemical nature of the
molecule.

3-25 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Functional Groups

3-26 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Macromolecules of Life

 Macromolecules are very large organic

molecules.
 The most important organic compounds
found in living things are:
– Carbohydrates
– Proteins
– Nucleic acids
– Lipids

3-27 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Synthesis of Macromolecules
OH H

Short polymer Monomer

Dehydration
H2O
reaction

Longer polymer
(a) Building a polymer chain
Breaking of Macromolecules
H2O

Hydrolysis

OH H

(b) Breaking a polymer chain

 Polymers

 Carbohydrates, proteins and nucleic acids are

polymers.
 Polymers are combinations of smaller building blocks.
– The building blocks are called monomers.
 Polymers are built via dehydration synthesis.
 Polymers are broken apart via hydrolysis.

3-30 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Carbohydrates

(a) Linear and ring structures (b) Abbreviated ring

structure
(CH2O)n
 OH H

Glucose Galactose

H2O

Lactose
 Polymers

3-33 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Complex Carbohydrates

3-34 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Carbohydrates

 Organic molecules composed of carbon, hydrogen

and oxygen
 All have the general formula CH2O
 Names end in –ose
 Serve as the primary energy source for most living
things
 Also serve as structural support
– Plant cell walls
 Important components of nucleic acids
– DNA and RNA

3-35 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Simple Sugars

 Simple sugars are described by the number

of carbons in the molecule.
– Triose-3 carbons
– Pentose-5 carbons
– Hexose-6 carbons
 Examples of simple sugars:
– Glucose
– Fructose
– Galactose
3-36 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Complex Carbohydrates

 When two or more simple sugars are

combined, they form complex carbohydrates.
– Formed via dehydration synthesis
 Disaccharides
– Two simple sugars
 Sucrose
 Lactose
 Maltose
 Trisaccharides
– Three simple sugars
3-37 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Polysaccharides

 Contain many simple sugars

 Examples of polysaccharides:
– Starch and glycogen
 Used for energy storage in plants (starch) and animals
(glycogen)
– Cellulose
 Important component of plant cell walls
 Humans cannot digest cellulose; it is the fiber in our diet.
– Helps facilitate movement of food through the digestive
tract

3-38 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Proteins

 Proteins are polymers

made of amino acids.
 An amino acid contains:
– Central carbon
– Amino group
– Carboxyl group
– Hydrogen
 There are 20 different
amino acids.

3-39 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 MAJOR TYPES OF PROTEINS
Structural Proteins Storage Proteins Contractile Transport Proteins Enzymes
(provide support) (provide amino Proteins (help transport (help chemical
acids for growth) (help movement) substances) reactions)
 Amino Carboxyl
group group

Side
chain

The general structure of an amino acid

Hydrophobic Hydrophilic
side chain side chain

Leucine Serine

Examples of amino acids with hydrophobic and hydrophilic

side chains
 Carboxyl Amino
group group

OH H

Side Side
chain chain
Amino acid Amino acid

Dehydration reaction
H2O

Side Side
chain chain

Peptide bond
 The Structure of Proteins

 Amino acids are joined via dehydration synthesis.

– The bond formed between amino acids is called a peptide
bond.
 Several amino acids joined together form
polypeptide chains.

3-45 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Primary Structure

 The sequence of amino acids in a polypeptide

constitutes the primary structure of the protein.
 This sequence is dictated by information in genes
(DNA).
 All levels of protein structure depend on the primary
sequence.

3-47 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
ALPHA HELIX
BETA STRAND and BETA SHEET
 Secondary Structure

 Polypeptides twist and fold

into their secondary structure.
– Some sequences of amino
acids twist into a helix.
 This is called an alpha helix.
– Some sequences of amino
acids remain straight and
fold back on themselves.
 This is called a beta-pleated
sheet.

3-50 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Myoglobin: An example of a tertiary structure
Myoglobin: An example of a tertiary structure
Examples of Protein tertiary structures
Hemoglobin: An example of a quaternary structure
 Tertiary Structure

 The various alpha

helices and beta
pleated sheets interact
to form a globular
structure.
 This globular structure
is unique for each
polypeptide.

3-55 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Quaternary Structure

 Some proteins contain more

than one polypeptide chain.
 Each of these polypeptides
has its own unique tertiary
structure.
– These polypeptides interact
to form a more complex
globular structure.
 Quaternary structure can be
stabilized by disulfide bonds.

3-56 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Form and Function

Sickle cell anemia

Normal
protein
Prion
Clusters
of prions

Skull
Prion Prion
converts proteins
Brain normal clump
proteins together

Bovine spongiform Kuru Fatal weight loss in

encephalopathy deer, elk, and moose
(BSE)
Prions
Binding mode between inhibitor and
HIV protease
 Proteins
 are polymers of amino acid monomers,
 account for more than 50% of the dry weight of most cells, and
 are instrumental in almost everything cells do.
• All proteins are made by stringing together a common set of 20 kinds of
amino acids.
• Every amino acid consists of a central carbon atom bonded to four
covalent partners.
• Three of those attachment groups are common to all amino acids:
1. a carboxyl group (COOH),
2. an amino group (NH2), and
3. a hydrogen atom.
©
• The variable component of amino acids
2016
Pear • is called the side chain and
son • is attached to the fourth bond of the central carbon.
• Each type of amino acid has a unique side chain, which gives that
Edu
cati amino acid its special chemical properties.
on,
Inc.
 Structure/Function: Protein Shape
 Cells link amino acids together by dehydration reactions,
– forming peptide bonds, and
– creating long chains of amino acids called polypeptides.
 A functional protein is one or more polypeptide chains precisely twisted, folded,
and coiled into a molecule of unique shape.

• How is it possible to make the huge variety of proteins found in your body from
just 20 kinds of amino acids?
• Like the English alphabet used to make different words by varying the
sequence of just 26 letters, proteins use 20 different “letters” (amino acids)
to create polypeptides hundreds or thousands of amino acids in length.

• The amino acid sequence of each polypeptide determines the three-dimensional

structure of the protein.
• A protein’s three-dimensional structure enables the molecule to carry out its
specific function.
• Nearly all proteins work by recognizing and binding to some other molecule.
 Structure/Function: Protein Shape
 A slight change in the amino acid sequence can affect a protein’s ability
to function.
 The substitution of one amino acid for another at a particular position in
hemoglobin, the blood protein that carries oxygen, causes sickle-cell
disease, an inherited blood disorder.
• A protein’s shape is sensitive to the environment. An unfavorable
change in temperature, pH, or some other factor can cause a protein to
unravel.

• One difference in sequence is enough to cause the protein to fold into a

© different shape, which alters its function, which in turn causes disease.
2016
• Misfolded proteins are associated with many diseases, including some
Pear
son severe nervous system disorders.
Edu
cati
on,
Inc.
 Form and Function
 The protein’s overall shape
determines its job.
 If a protein is not shaped
properly, it likely will not work
properly.
 Example:
– Sickle cell anemia
– A mutation in the gene causes
the protein to have a different
shape.
– This shape change results in a
change in function.
 Denaturation:
– When heat or other
environmental conditions break
the bonds that stabilize tertiary
structure.

3-65 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Nucleic Acids

 The largest biological

molecules
 Store and transfer
information within a cell
 Include DNA and RNA
 Are made of
nucleotides
– 5-carbon sugar
– Phosphate group
– Nitrogenous group
3-67 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Nitrogenous base
(can be A, G, C, or U/T)

Connection to the next

nucleotide in the chain

Uracil (U)

Phosphate
group

Sugar (deoxy)
ribose

Connection to the next

nucleotide in the chain
 Components of Nucleotides
5-carbon sugar

DNA RNA
 Components of Nucleotides

Nitrogenous
base * *
T
A DNA

G
RNA
Nitrogen attaches
* with sugar molecule
C U
 Nitrogenous base
(can be A, G, C, or T)
Connection
to the next
nucleotide
in the chain

Thymine (T)

Phosphate
group Phosphate
Base

Sugar
Connection to the (deoxyribose)
next nucleotide in Sugar
the chain
 Sugar-phosphate
backbone

Base
Nucleotide pair
Hydrogen
bond

Bases

(b) Double helix

(a) DNA strand (two polynucleotide strands)
(polynucleotide) Space-filling model of DNA
 The Structure of DNA

3-73 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 DNA

 Each DNA molecule is made of two strands.

– Held together by hydrogen bonds between the nitrogenous
bases
– The bases pair according to base pair rules.
 Adenine - thymine
 Cytosine - guanine
 The two DNA strands are twisted on each other, forming
a double helix.
 Each DNA strand is divided into segments.
– Each segment forms a gene.
– Genes are the recipes for proteins.
 The sequence of nucleotides in a gene dictate the order of amino
acids in a polypeptide.
3-74 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 DNA and Chromosomes

 Each DNA strand has many genes.

 Each DNA strand is called a chromosome.
 Human cells have 46 chromosomes in each
cell.
– Each cell copies all of these chromosomes before
it divides to pass along to daughter cells.

3-75 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 The Functions of DNA

3-76 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 The Functions of DNA

 DNA is able to:

– Replicate itself
– Store information and transmit it to offspring
– Direct synthesis of proteins
– Mutate (change chemically)

3-77 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 RNA

 RNA is a single-stranded molecule.

 Contains uracil instead of thymine
 Base pairs with itself and DNA
– A-U
– G-C
 RNA is found in three different forms:
– mRNA (messenger RNA)
– rRNA (ribosomal RNA)
– tRNA (transfer RNA)

3-78 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 DNA
vs.
RNA

3-80 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Lipids

 Commonly called fats

 Large and nonpolar
– Do not dissolve in water
– Dissolve in other nonpolar molecules like acetone
 Usually have very few oxygen atoms
 There are three main types of lipids:
– True fats (e.g., pork chop fat and oils)
– Phospholipids (membrane components)
– Steroids (most hormones)

3-81 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 H HO
Fatty acid

H2O

Glycerol

A dehydration reaction linking a fatty acid to glycerol

A fat molecule with a glycerol “head” and three
energy-rich hydrocarbon fatty acid “tails”
 True (neutral) Fats

 Used to provide energy

 The building blocks of
fats
– A glycerol molecule
– Three fatty acids

3-84 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Saturated vs. Unsaturated Lipids

 If the carbon skeleton of a fatty acid has as much

hydrogen as possible, the fat is called a saturated fat.
– Saturated fats are found in animal tissues and tend to be
solid at room temperature.
 If the carbons of a fat have double-bonded carbon
molecules in them, the fat is called unsaturated fat.
– Unsaturated fats are frequently plant fats and are liquids at
room temperature.
– A polyunsaturated fat has several double bonds.
– Fats are important energy storage molecules.

3-85 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Saturated and Unsaturated
Fatty Acids

3-86 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Phospholipids

 Are complex organic

molecules that
resemble fats but
contain phosphate
groups
 Phospholipids are the
major components of
cell membranes.

3-87 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Steroids
 Steroids

 Nonpolar molecules that are arranged in rings of

carbon
 Steroids are important components of cell
membranes.
– Cholesterol
 Steroids often serve as hormones and serve in
regulation of body processes.
– Testosterone, estrogen

3-89 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Overview

3-90 Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.