Chemistry-part 3

Chapter 2 (2.4)
Chapter 4 (4.1)

Levels of Organization:
◼ Atomic

◼ Molecular→
Macromolecules
◼ Cellular
◼ Tissue
◼ Organ
◼ Organ System
◼ Organism

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 Biochemistry
◼ Organic compounds- Contain carbon, Contain
covalent bonds; Molecules unique to living
organisms contain carbon and hence are
organic compounds
◼ Inorganic compounds- Do not contain carbon,
Ex) water, salts, many acids & bases

Biochemistry
◼ Since organic compounds are often large,
interactions with other molecules often
involve only small, reactive parts called
functional groups– 5 important functional
groups shown in figure 2.14

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◼ All living things are made up of 4 classes of macromolecules:
1) carbohydrates
2) lipids
3) proteins
4) nucleic acids

◼3 of 4 classes of life’s macromolecules are

polymers: a long molecule consisting of
many similar building blocks called
monomers; An immense variety of
polymers can be built from a small set of
monomers

Synthesis & Breakdown of macromolecules

◼ A dehydration synthesis reaction (or
condensation reaction) occurs when 2
monomers bond together through the loss
of a water molecule
◼ Polymers are disassembled to monomers
by hydrolysis, a reaction that is essentially
the reverse of the dehydration reaction

1) Carbohydrates
◼ Carbohydrates usually serve as fuel & building material
◼ Monosaccharides: (single sugars)- simplest
carbohydrates; have molecular formulas that are
usually multiples of CH2O
◼ Glucose is most common & important fuel = C6H12O6
◼ Ribose & Deoxyribose are important for nucleic acids

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 1) Carbohydrates
◼ dehydration
reaction creates a glycosidic linkage
between monosaccharides → Disaccharides
◼ →Oligosaccharides
◼ → Polysaccharides

Polysaccharides:
polymers of sugars,
have storage &
structural roles;
◼ Starch- storage
polysaccharide of
plants
◼ Glycogen-
storage
polysaccharide in
animals, differs
from starch in
degree of
branching

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Polysaccharides: continued
◼ Cellulose- a major component of
plant walls, not digestible by
humans

1) Carbohydrates
Conjugated carbohydrates:
◼ glycolipid- lipid covalently bonded
to chains of sugars
(carbohydrates)
◼ glycoprotein- protein covalently
bonded to chains of sugars
(carbohydrates)
◼ proteoglycan- similar to
glycoprotein, but carbohydrate is
dominant with a smaller protein
bound to it

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 2) Lipids
◼ The one class of macromolecules that do not form polymers
◼ Usually composed of C, H, O (H>>>O)
◼ More variable in structure than the other 3 macromolecules; key feature of
lipids is that they are hydrophobic
◼ The 5 most biologically important lipids are:
a) Fatty Acids
b) Triglycerides
c) Phospholipids
d) Steroids
e) Eicosanoids

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a) Fatty acids: vary in length & in the # and

locations of double bonds
◼ Saturated fatty acids: have maximum # of
hydrogen atoms possible & no double bonds C
C
◼ Unsaturated fatty acids: have one or more double
bonds; polyunsaturated?
trans-fatty acid VS cis-fatty acid

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b) Triglycerides
(triacylglycerols;
neutral fats):
◼ 3 fatty acids
joined by ester
linkages to 1
Glycerol
◼ major function is
energy storage
(insulation &
cushioning) in
adipose cells

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2) Lipids
b) Triglycerides
(triacylglycerols;
neutral fats):
◼ Saturated fats VS
Unsaturated fats-?

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 2) Lipids
c) Phospholipids: composed of 2 fatty acids
& a phosphate group attached to glycerol
“backbone” by ester linkages
◼ Amphiphilic- partly non-polar (hydrophobic
“tails”), partly polar (hydrophilic “head”)
◼ major component of all cell membranes
◼ When phospholipids are added to water, they
self-assemble into a bilayer, with the
hydrophobic tails pointing toward the interior
→ results in a bilayer arrangement found in
cell membranes

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2) Lipids
d) Steroids:
◼ carbon skeleton consisting of 4
fused rings
◼ Cholesterol, an important “parent”
steroid from which other steroids are
synthesized & an important
component in cell membranes
◼ Cortisol, progesterone, estrogens,
testosterone, bile acids

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 2) Lipids
e) Eicosanoids: compounds with 20 C
◼ Function primarily as chemical
signals between cells
◼ Includes prostaglandins- 5 C ring;
function in variety of signaling roles
including inflammation, blood
clotting, hormone action, labor
contractions, blood vessel diameter

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3) Proteins
◼ >50% of the dry
mass of cells
◼ A protein is a
polymer of amino
acids monomers-
linked by peptide
bonds
◼ Peptides named for
# of amino acids:
 Dipeptides
 Tripeptides
 Oligopeptides
 Polypeptides
 Proteins

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 3) Proteins
◼ Amino acids- consists of a
central carbon with 4 groups
attached to it:
 a Hydrogen
 a carboxyl group (COOH)
 an amino group (NH2)
 a unique “R” group
◼ Amino acids differ in their
properties due to different side
chain R groups

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3) Proteins

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◼ Each polypeptide has a unique linear
sequence of amino acids which determines
a protein’s 3-D structure; its conformation
◼ A functional protein consists of one or
more polypeptides twisted, folded, & coiled
into a unique shape→ a protein’s structure
determines its function

Four Levels of Protein Structure:

◼ Primary structure
◼ Secondary structure
◼ Tertiary structure
◼ Quaternary structure

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3) Proteins
◼ Primary structure: unique linear
sequence of amino acids in a protein;
determined by inherited genetic
information (DNA)

◼ Secondary structure: consists of

localized coils & folds in polypeptide
chain; found in most proteins (but not all)
◼ The coils & folds of secondary structure
result from hydrogen bonds between
repeating components of the polypeptide
backbone
◼ 2 of the most common secondary
structures are:
 helix- coil
 pleated sheet- folded structure

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 3) Proteins
◼ Tertiary
structure:
determined by
interactions
between R
groups

◼ Quaternary structure: results

when 2 or more polypeptide chains
form one macromolecule
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3) Proteins
◼A slight change in primary structure can affect a protein’s higher structures &
ability to function; EX- Sickle-cell disease, an inherited blood disorder, results
from a single amino acid substitution in the protein hemoglobin

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 3) Proteins

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◼ Reactions require a certain amount of energy be absorbed to “prime” the reaction-

Activation Energy: amount of energy required to break bonds of reactants so they can
rearrange themselves to form product
◼ Enzymes catalyze reactions by decreasing amount of activation energy required

Mechanism of Enzyme Action:

1) Active site of enzyme (E) binds with substrate (S)
2) The enzyme-substrate complex (E-S) undergoes internal arrangements–
product is formed at a lower activation energy
3) Enzyme releases product

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 3) Proteins
◼ Alterations in pH, salt
concentration, temperature,
or other environmental
factors can cause a protein
to unravel: denaturation
◼ a denatured protein is
biologically inactive
◼ Sometimes denaturation is
reversible, but often it is not
and therefore permanently
destroys protein function

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4) Nucleic Acids
◼ largest molecules in body: store & transmit hereditary information
◼ composed of C, O, H, N, P
◼ 2 major classes:
Deoxyribonucleic
acid (DNA) &
Ribonucleic acid
(RNA)
◼ Nucleotide:
structural unit,
composed of 3
parts:
 5-carbon sugar
 1 or more
phosphate
groups
 1 of 5 Nitrogen-
containing
base groups

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 4) Nucleic Acids
◼ Nucleic acids are
polymers
(polynucleotides)
made of monomers:
nucleotides
◼ Nucleotides are linked
together to build a
polynucleotide by
dehydration synthesis
to form
phosphodiester bond
between pentose
sugar of 1 nucleotide
& phosphate group on
next nucleotide
◼ These links create a
backbone of sugar-
phosphate units with
nitrogenous bases as
appendages

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4) Nucleic Acids
◼ Adenosine Triphosphate
(ATP)- body’s most important
energy-transfer molecule;
composed of nitrogenous base
adenine, a ribose sugar, & 3
phosphate groups; very unstable;
phosphate groups can be
removed by hydrolysis & energy
is released

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Learning Objectives
When you have completed this section, you should be able to:
◼ Explain why carbon is especially well suited to serve as the structural
foundation of many biological molecules; define organic molecules
◼ Identify the 5 most common functional groups found in organic molecules
◼ Name the 4 major macromolecules of the body & describe their major
structural features & major functions in the body
◼ Discuss the relevance of polymers to biology and explain how they are
formed and broken by dehydration synthesis & hydrolysis
◼ Name the monomers (or components), polymers (or larger molecule), & types
of bonds found in these polymers for of each of the 4 macromolecules
◼ Discuss the types and functions of carbohydrates
◼ Discuss the types and functions of lipids
◼ Discuss protein structure and function; explain denaturation & its importance
◼ Explain how enzymes function
◼ Identify the principal types of nucleic acids & describe their major structural
components
◼ Describe the structure and function of ATP

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