Module 2 The Chemical Basis of Life
Module 2 The Chemical Basis of Life
The Chemical
Basis of Life
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
Matter
Fig. 2.2
Identification of Elements
• Atomic number: equal to the number of
protons
• Mass number: equal to the mass of the
protons and neutrons
• Atomic weight: average of the mass
numbers of all isotopes
• Isotope: atoms with same number of
protons but a different number of neutrons
Chemical Bonds
Fig. 2.4
Polar and Nonpolar Molecules
• Electrons shared
equally between
atoms produce
nonpolar molecules
• Unequal sharing of
electrons produces
polar molecules
Fig. 2.5
Hydrogen Bonds
Figure 2.10a
Molecules and Compounds
Fig. 2.8
Decomposition Reaction
• Breakdown of larger reactants into smaller
products
– Hydrolysis reaction: a decomposition reaction that
uses water
Fig. 2.8
Reversible Reactions
Fig. 2.9
Fig. 2.10
Factors Influencing Rate of Chemical Reactions
• Ranges from 0 to 14
• Indicates the H+ concentration of a solution
– Neutral solutions have an equal number of H+
and OH– and a pH of 7.0
– Acidic solutions have more H+ than OH– and a
pH of less than 7.0
– Basic (alkaline) solutions have fewer H+ than
OH– and a pH greater than 7.0
pH Scale
• Neutral: pH 7.00
• Acidic: pH 0–6.99
• Basic: pH 7.01–14.00
Fig. 2.11
Acids and Bases
• Salts are formed by the reaction of an acid and a
base
HCl + NaOH → NaCl + H2O
b) In a buffered solution
the added H+ is bound
by the buffer and the
pH change is much
smaller
Fig. 2.12
Biochemistry
• Inorganic chemistry
– Mostly concerned with non-carbon-containing
substances but does include such carbon-
containing substances as CO (Carbon
monoxide), CO2 (Carbon Doixide), and HCO3-
(Bicarbonate)
• Organic chemistry
– Substances contain carbon, are covalently
bonded, and are often large
– Usually have carbon-carbon or carbon-hydrogen
bonding
Inorganic Compounds
Figure 2.14a
Fig. 2.13
Lipids
• Dissolve in nonpolar solvents, such as alcohol or
acetone, but not in polar solvents, such as water
• Contain C, H, and O, but the proportion of
oxygen in lipids is less than in carbohydrates
• Examples:
– Fats or triglycerides: energy
– Phospholipids: structural components of cell
membranes
– Eicosanoids: regulate physiological processes
– Steroids: regulate physiological processes
Examples of Lipids Found in the Body
Fig. 2.14
Fatty Acids
• Saturated: only single covalent bonds between carbons
• Unsaturated: one or more double covalent bonds
between carbons
Fig. 2.15
Other Lipids
• Phospholipids: modified triglycerides with two
fatty acid groups and a phosphorus group
Fig. 2.16
Other Lipids
• Eicosanoids: 20-carbon fatty acids found in cell
membranes
• Steroids: flat molecules with four interlocking
hydrocarbon rings
Fig. 2.17
Proteins
• Macromolecules
• Contain C, H, O, N, and some S
• Composed of 20 basic types of amino
acids bound together with peptide bonds
– Dipeptide: Two amino acids
– Tripeptide: Three amino acids
– Polypeptide: Many amino acids
• Proteins are polypeptides of hundreds of
amino acids
Amino Acids (AA)
• Building blocks of
proteins
• Organic acids
containing
– amino group (-NH2)
– a carboxyl group (COOH)
– a hydrogen atom
– a side chain designated by
the symbol R attached to the
same carbon atom as the
hydrogen
Structural Levels of Proteins
• Primary: determined by the number, kind, and
arrangement of amino acids
• Secondary: results from folding or bending of
the polypeptide chain caused by the hydrogen
bonds between amino acids (helices and pleated
sheets)
• Tertiary: results from the folding of the helices or
pleated sheets and the hydrogen bonds formed
with water
• Quaternary: spatial relationships between two
or more proteins that associate to form a
functional unit
Fig.
2.19ab
Fig.
2.19cd
Proteins
• Functions
– regulate chemical reactions (enzymes)
– structural proteins provide the framework for many of the
body’s tissues
– responsible for muscle contraction
– Fibrous proteins
• Extended and strand-like proteins
• Examples: keratin, elastin, collagen, and certain contractile fibers
– Globular proteins
• Compact, spherical proteins with tertiary and quaternary structures
• Examples: antibodies, hormones, and enzymes
• Denaturation
– Disruption of hydrogen bonds, which changes the shape of
proteins and makes them nonfunctional
Characteristics of Enzymes
• Speed up chemical reactions by lowering the
activation energy
• Most are globular proteins that act as biological
catalysts
• Are chemically specific
• Frequently named for the type of reaction they
catalyze
• Names usually end in -ase
• Chemical events of the body are regulated
primarily by mechanisms that control
– concentration of enzymes
– activity of enzymes
Fig. 2.20
Enzymes
• Enzymes bind to
reactants according to the
lock-and-key model
– The shape of both the
enzyme and reactants are
critical to the function of the
enzyme
– By bringing the two reactants
close to each other it reduces
the activation energy for the
reaction
– Each enzyme catalyzes only
one type of chemical reaction
– After each reaction the
enzyme is released and can
be used again
Fig. 2.21
Nucleic Acids
• Composed of C, O, H, N, and P
• The basic unit of nucleic acids is the
nucleotide, which is a monosaccharide with
an attached phosphate and organic base
• Five nitrogenous bases contribute to
nucleotide structure:
– adenine (A)
– guanine (G)
– cytosine (C)
– thymine (T)
– uracil (U)
• Two major classes: DNA and RNA
Deoxyribonucleic Acid (DNA)
• Double-stranded helical molecule found in the
nucleus of the cell
• Genetic material of the cell
• Replicates itself before the cell divides, ensuring
genetic continuity
• Provides instructions for protein synthesis
• Contains the monosaccharide deoxyribose and
the organic bases
– adenine
– thymine
– guanine
– cytosine
Fig. 2.22
Ribonucleic Acid (RNA)