proteins

Amino acid: Basic unit of protein

R
Different side chains,
- R, determin the
NH3 +
C COO properties of 20
Amino group Carboxylic
acid group amino acids.
H
An amino acid
 20 Amino acids

Glycine (G) Alanine (A) Valine (V) Isoleucine (I) Leucine (L)

Proline (P) Methionine (M) Phenylalanine (F) Tryptophan (W) Asparagine (N)

Glutamine (Q) Serine (S) Threonine (T) Tyrosine (Y) Cysteine (C)

Asparatic acid (D) Glutamic acid (E) Lysine (K) Arginine (R) Histidine (H)

White: Hydrophobic, Green: Hydrophilic, Red: Acidic, Blue: Basic

One group of amino acids has hydrophobic R groups.
Another group of amino acids has polar R
groups, making them hydrophilic.
• The last group of amino acids includes those with
functional groups that are charged (ionized) at
cellular pH.
• Some R groups are bases, others are acids.
 Proteins

• Classification of amino acids

- Essential (egzogenne np. metionina)
- Nonessential (endogenne np. alanina)
• Amino acids are joined together when a
dehydration reaction removes a hydroxyl group
from the carboxyl end of one amino acid and a
hydrogen from the amino group of another.

• The resulting covalent bond is called a peptide bond.

Peptide Bonds

9
 Peptide Bond Formation
• Individual amino acids form a polypeptide chain
• Such a chain is a component of a hierarchy for describing
macromolecular structure
• The chain has its own set of attributes

Primary Structure PHAR201 Lecture 1 2012 10

 Levels of Protein Structure
1. Primary structure
2. Secondary structure
3. Tertiary structure
 are used to organize the folding within a single
polypeptide.
4. Quarternary structure arises when two or
more polypeptides join to form a protein.
• The primary structure of a
protein is its unique
sequence of amino acids.
– Lysozyme, an enzyme
that attacks bacteria,
consists on a
polypeptide chain of 129
amino acids.
– The precise primary
structure of a protein is
determined by inherited
genetic information.
• The secondary structure of a protein results from
hydrogen bonds at regular intervals along the
polypeptide backbone.
– Typical shapes
that develop from
secondary structure
are coils (an alpha
helix) or folds
(beta pleated
sheets).
• The structural properties of silk are due to beta
pleated sheets.
– The presence of so many hydrogen bonds makes each silk
fiber stronger than steel.
 SECONDARY STRUCTURE
The folding of the N-C-C
backbone of the
polypeptide chain using
weak hydrogen bonds

© Text 2007 Paul Billiet ODWS

© Science Student
 SECONDARY STRUCTURE
• This produces the alpha helix and beta pleating

© Text2007 Paul Billiet ODWS

© Dr Gary Kaiser
 TERTIARY STRUCTURE
The folding of the polypeptide into domains
whose chemical properties are determined by
the amino acids in the chain

MIL1 protein

© 2007 Paul Billiet ODWS

© Anne-Marie Ternes
Three-dimensional structure of proteins

Tertiary structure

Quaternary structure
 TERTIARY STRUCTURE
• This folding is sometimes held together by strong
covalent bonds
(e.g. cysteine-cysteine disulphide bridge)
• Bending of the chain takes place at certain amino
acids
(e.g. proline)
• Hydrophobic amino acids tend to arrange
themselves inside the molecule
• Hydrophilic amino acids arrange themselves on the
outside

© 2007 Paul Billiet ODWS

• Tertiary structure is determined by a variety of
interactions among R groups and between R groups
and the polypeptide backbone.
– These interactions
include hydrogen
bonds among polar
and/or charged
areas, ionic bonds
between charged
R groups, and
hydrophobic
interactions and
van der Waals
interactions among
R groups.
• Quarternary structure
results from the aggregation
of two or more polypeptide
subunits.
– Collagen is a fibrous protein
of three polypeptides that are
supercoiled like a rope.
• This provides the structural
strength for their role in
connective tissue.
– Hemoglobin is a
globular protein
with two copies
of two kinds
of polypeptides.
• A protein’s conformation can change in response to
the physical and chemical conditions.
• Changes in pH, salt concentration, temperature, or
other factors can unravel or denature a protein.
– These forces disrupt the hydrogen bonds, ionic bonds, and
disulfide bridges that maintain the protein’s shape.
• Some proteins can return to their functional shape
after denaturation, but others cannot, especially in
the crowded environment of the cell.
– Usually denaturation is permanent
 Hierarchical nature of protein structure
Primary structure (Amino acid sequence)
↓
Secondary structure （ α-helix, β-sheet ）
↓
Tertiary structure （ Three-dimensional structure
formed by assembly of secondary structures ）
↓
Quaternary structure （ Structure formed by more
than one polypeptide chains ）
 Proteins Come In Many Varieties!
• Proteins include a diversity of structures,
resulting in a wide range of functions

• Proteins account for more than 50% of the dry

mass of most cells

• Protein functions include structural support,

storage, transport, cellular communications,
movement, and defense against foreign
substances

28
 Enzymatic

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

Enzyme

29
 Storage
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.

Amino acids
Ovalbumin for embryo

30
 Structural

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
 Receptor

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

32
 Transport
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

33
 Defensive

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

Antibodies

Virus Bacterium

34
 Hormonal

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

35
 Types of Proteins
• Globular Proteins – most of what we have
dealt with so far
– Compact shape like a ball with irregular
surfaces
– Enzymes are globular
• Fibrous Proteins – usually span a long
distance in the cell
– 3-D structure is usually long and rod shaped
• PROTEINS
a) Simple (białka proste)
b) Compound ( białka złożone)
• Proteins
a) Complete (animal proteins)-Białko
pełnowartościowe
b) Incomplete (plant proteins)-Białko
niepełnowartościowe