General Biology

BIOL 204
Lecture 4
 Objectives (learning outcomes)

At the end of this lecture the student will be able to:

A Preview of Cell Biology
List the functions of proteins.
Describe the structure of amino acids and proteins.
Define nucleic acids and explain their biological importance.
Describe the types and structure of nucleotides.
Differentiate between DNA and RNA.
 Enrichment Link:

Protein structure and function:

https://www.youtube.com/watch?v=wvTv8TqWC48

Gene expression:
https://www.youtube.com/watch?v=gG7uCskUOrA
All the large molecules that we know, found in the living
organisms, can be one of four categories:
Carbohydrates
lipids
proteins
Nucleic acids
The structure of large molecules is related to its function.
 Unit 5 / Concept 5.4

I- Proteins: a diversity of structures, resulting in

a wide range of functions
Every dynamic function of a living being depends on proteins.
“Protein” comes from the Greek word proteios meaning
“first”.
Proteins account for more than 50% of the dry mass of most
cells.
They are instrumental in almost everything organisms do:
chemical reactions, defense, storage, transport, cellular
communication, movement, or structural support.
 Unit 5 / Concept 5.4

An overview of protein functions.

Enzymatic proteins
Function: Selective acceleration of chemical reactions
Example: Digestive enzymes catalyze the hydrolysis
of bonds in food molecules.

Enzyme
 Unit 5 / Concept 5.4

An overview of protein functions.

Storage proteins
Function: Storage of amino acids
Examples: Casein, the protein of milk, is the major
source of amino acids for baby mammals. Plants have
storage proteins in their seeds. Ovalbumin is the
protein of egg white, used as an amino acid source
for the developing embryo.

Ovalbumin Amino acids

for embryo
 Unit 5 / Concept 5.4

An overview of protein functions.

Hormonal proteins
Function: Coordination of an organism’s activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up glucose,
thus regulating blood sugar concentration

Insulin
High secreted Normal
blood sugar blood sugar
 Unit 5 / Concept 5.4

An overview of protein functions

Contractile and motor proteins

Function: Movement
Examples: Motor proteins are responsible for the
undulations of cilia and flagella. Actin and myosin
proteins are responsible for the contraction of
muscles.

Actin Myosin

Muscle tissue
100 m
 Unit 5 / Concept 5.4

An overview of protein functions.

Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help destroy
viruses and bacteria.

Antibodies

Virus Bacterium
 Unit 5 / Concept 5.4

An overview of protein functions.

Transport proteins
Function: Transport of substances
Examples: Hemoglobin, the iron-containing protein of
vertebrate blood, transports oxygen from the lungs to
other parts of the body. Other proteins transport
molecules across cell membranes.

Transport
protein

Cell membrane
 Unit 5 / Concept 5.4

An overview of protein functions.

Receptor proteins
Function: Response of cell to chemical stimuli
Example: Receptors built into the membrane of a
nerve cell detect signaling molecules released by
other nerve cells.

Receptor
Signaling protein
molecules
 Unit 5 / Concept 5.4

An overview of protein functions.

Structural proteins
Function: Support
Examples: Keratin is the protein of hair, horns, feathers,
and other skin appendages.
Insects and spiders use silk fibers to make their cocoons
and webs, respectively.
Collagen and elastin proteins provide a fibrous framework
in animal connective tissues.

Collagen

Connective
tissue 60 m
 Unit 5 / Concept 5.2

A polypeptide is a polymer constructed from the same set of

20 amino acids.
The bond between amino acids is called a peptide bond.
A protein is a biologically functional molecule made up of
one or more polypeptides.
 Unit 5 / Concept 5.4

1- Amino Acid Monomers

An amino acid is an organic molecule with an amino group, a
carboxyl group, a hydrogen atom, and a variable group
symbolized by R.
The R group, also called the side chain, differs with each amino
acid.
Side chain (R group)

Amino acid monomer

Amino Carboxyl
group group
 Unit 5 / Concept 5.4

The amino acids are grouped according to the properties of their side chain:

a- Nonpolar side chains; hydrophobic

Side chain

Glycine Alanine Valine Leucine Isoleucine

(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)

Methionine Phenylalanine Tryptophan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)
 Unit 5 / Concept 5.4

The amino acids are grouped according to the properties of their side chain:
b- Polar side chains; hydrophilic

Serine Threonine Cysteine

(Ser or S) (Thr or T) (Cys or C)

Tyrosine Asparagine Glutamine

(Tyr or Y) (Asn or N) (Gln or Q)
 Unit 5 / Concept 5.4

The amino acids are grouped according to the properties of their side chain:

c- Electrically charged side chains; hydrophilic

Basic (positively charged)

Acidic (negatively charged)

Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
 Unit 5 / Concept 5.4

Polypeptides (Amino Acid Polymers)

Amino acids are linked by peptide bonds.
Polypeptides range in length from a few amino acids to
1,000 or more.
Each specific polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and an
amino end (N-terminus).
 Unit 5 / Concept 5.4

Making a polypeptide chain

Peptide bond

New peptide
bond forming

Side
chains

Back-
bone

Amino end Peptide Carboxyl end

(N-terminus) bond (C-terminus)
 Unit 5 / Concept 5.4

Protein Structure and Function

A functional protein consists of one or more polypeptides

precisely twisted, folded, and coiled into a unique shape.

The sequence of amino acids determines a protein’s

three-dimensional structure.

A protein’s structure determines its function.

 Unit 5 / Concept 5.4

Four Levels of Protein Structure

1- The primary structure of a protein is its unique sequence
of amino acids
2- Secondary structure, found in most proteins, consists of
coils and folds in the polypeptide chain.
3- Tertiary structure is determined by interactions among
various side chains (R groups)
4- Quaternary structure results when a protein consists of
multiple polypeptide chains
 Unit 5 / Concept 5.4

Primary structure

Amino
acids

Amino end

Primary structure of transthyretin

Carboxyl end
 Unit 5 / Concept 5.4

Secondary, Tertiary and quaternary structure

Quaternary
structure
Secondary Tertiary
structure structure

helix

Hydrogen bond
pleated sheet
strand
Transthyretin
Hydrogen Transthyretin protein
bond polypeptide
 Unit 5 / Concept 5.4

What Determines Protein Structure?

In addition to primary structure, physical and chemical
conditions can affect structure.

Alterations in pH, salt concentration, temperature, or

other environmental factors can cause a protein to unravel.

This loss of a protein’s native structure is called

denaturation.

A denatured protein is biologically inactive.

 Unit 5 / Concept 5.4

Denaturation and renaturation of a protein

tu

Normal protein Denatured protein

 Unit 5 / Concept 5.5

II- Nucleic acids store, transmit, and help express

hereditary information

Nucleic acids are polymers made of monomers called

nucleotides.

The two types of nucleic acids are:

Deoxyribonucleic acid (DNA)

Ribonucleic acid (RNA).

 Unit 5 / Concept 5.5

The Roles of Nucleic Acids

DNA is the genetic material that organisms inherit from
their parents.

DNA provides directions for its own replication.

DNA directs RNA synthesis.

DNA controls protein synthesis through RNA: this process

is called gene expression.
 Unit 5 / Concept 5.5
DNA

1 Synthesis of
mRNA
mRNA

NUCLEUS
Gene expression:
CYTOPLASM
DNA ---- RNA ---- protein
mRNA
2 Movement of
mRNA into Ribosome
cytoplasm

3 Synthesis
of protein

Amino
Polypeptide acids
 Unit 5 / Concept 5.5

The Components of Nucleic Acids

Nucleic acids are polymers of nucleotides called polynucleotides.
Nucleotide = nitrogenous base + sugar + phosphate group

Nucleoside
Nitrogenous
base

5C

Phosphate 3C
group Sugar
(pentose)
Nucleotide
Nucleoside = nitrogenous base + sugar
 Unit 5 / Concept 5.5

There are two families of nitrogenous bases:

Nitrogenous bases
Pyrimidines

Pyrimidines (cytosine,
thymine, and uracil) have a
single six-membered ring.
Cytosine Thymine Uracil
(C) (T, in DNA) (U, in RNA)

Purines (adenine and guanine) Purines

have a six-membered ring
fused to a five-membered
ring.

Adenine (A) Guanine (G)

 Unit 5 / Concept 5.5

In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose.

Sugars

Deoxyribose Ribose
(in DNA) (in RNA)
 Unit 5 / Concept 5.5

5C Nucleotide Polymers
3C Adjacent nucleotides are joined by covalent
bonds that form between the —OH group
5C
on the 3 carbon of one nucleotide and the
3C
phosphate on the 5 carbon on the next.

5C
These links create a backbone of sugar-

3C
phosphate units with nitrogenous bases as
appendages.
5C The sequence of bases along a DNA or
3C mRNA polymer is unique for each gene.

Polynucleotide, or nucleic acid

 Unit 5 / Concept 5.5

The Structures of DNA and RNA Molecules

• RNA molecules usually exist as single polypeptide chains.

• DNA molecules have two polynucleotides spiraling around

an imaginary axis, forming a double helix.

• In the DNA double helix, the two backbones run in opposite

5 → 3 directions from each other, an arrangement referred
to as antiparallel.

• One DNA molecule includes many genes.

 Unit 5 / Concept 5.5

The nitrogenous bases in DNA pair up and form hydrogen

bonds: adenine (A) always with thymine (T), and guanine
(G) always with cytosine (C) Called complementary base
pairing.
Complementary pairing can also occur between two RNA
molecules or between parts of the same molecule.
In RNA, thymine is replaced by uracil (U) so A and U pair.
 Unit 5 / Concept 5.5

5 3 Sugar-phosphate
backbones
Hydrogen bonds

Base pair joined

by hydrogen
bonding

3 5 Base pair joined

by hydrogen bonding
DNA Transfer RNA
The End