PROTEINS

Characteristics of Proteins
• Contain carbon, hydrogen, oxygen,
nitrogen, and sulfur
• Serve as structural components of animals
• Serve as control molecules (enzymes)
• Serve as transport and messenger
molecules
• Basic building block is the amino acid
 Amino Acid

• Amine group acts like a base, tends to be positive.

• Carboxyl group acts like an acid, tends to be negative.
• “R” group is variable, from 1 atom to 20.
• Two amino acids join together to form a dipeptide.
• Adjacent carboxyl and amino groups bond together.
Some Amino Acids
Some More Amino Acids
Still More Amino Acids
Animation:
http://www.biotopics.co.uk/as/aminoco
 Amino Acid + Amino Acid --> Dipeptide

Amino Acid + Dipeptide --> Tripeptide

A.A. + A.A. + …..+ Tripeptide --> Polypeptide

A protein consists of one or more
polypeptide chains.
7.3.U7 The sequence and number of amino acids in the polypeptide is the primary structure. AND 7.3.U8 The secondary
structure is the formation of alpha helices and beta pleated sheets stabilized by hydrogen bonding. AND 7.3.U9 The
tertiary structure is the further folding of the polypeptide stabilized by interactions between R groups. AND 7.3.U10 The
quaternary structure exists in proteins with more than one polypeptide chain.

The four levels of protein structure. The level a protein conforms to is

determined by it’s amino acid sequence.

(Polypeptide) • The chains of amino acids fold or • The polypeptide folds and • The interaction
• The order / sequence of the amino turn upon themselves coils to form a complex between multiple
acids of which the protein is • Held together by hydrogen bonds 3D shape polypeptides or
composed between (non-adjacent) amine (N- • Caused by interactions prosthetic groups
• Formed by covalent peptide bonds H) and carboxylic (C-O) groups between R groups (H- • A prosthetic group
between adjacent amino acids • H-bonds provide a level of bonds, disulphide bridges, is an inorganic
• Controls all subsequent levels of structural stability ionic bonds and compound
structure • Fibrous proteins hydrophilic / hydrophobic involved in a
interactions) protein (e.g. the
• Tertiary structure may be heme group in
n.b. although you don’t need to be able to outline the different important for the function haemoglobin)
levels of structure for knowing of them helps to understand the (e.g. specificity of active • Fibrous and
difference between globular and fibrous proteins. This is though site in enzymes) Globular proteins
• Globular proteins
required knowledge for AHL (7.3.U7 to 7.3.U10)
 2.4.U6 The amino acid sequence determines the three-dimensional conformation of a protein.

Proteins are commonly described as either

being fibrous or globular in nature.
Fibrous proteins have structural roles whereas globular
proteins are functional (active in a cell’s metabolism).

In globular proteins the hydrophobic R groups are folded into the core of the molecule,
away from the surrounding water molecules, this makes them soluble. In fibrous proteins
the hydrophobic R groups are exposed and therefore the molecule is insoluble.
 2.4.U7 Living organisms synthesize many different proteins with a wide range of functions.

Usage of proteins Nothing can compare with the versatility of

proteins. Their functionality and usage in
Function organisms is unrivalled.
Description Key examples
There are thousands of different enzymes to catalyse specific
Catalysis Rubisco
chemical reactions within the cell or outside it.
Actin and myosin together cause the muscle contractions used
Muscle contraction
in locomotion and transport around the body.
Tubulin is the subunit of microtubules that give animals cells
Cytoskeletons
their shape and pull on chromosomes during mitosis.
Tensile Fibrous proteins give tensile strength needed in skin, tendons,
collagen
strengthening ligaments and blood vessel walls.
Plasma proteins act as clotting factors that cause blood to turn
Blood clotting
from a liquid to a gel in wounds.
Transport of Proteins in blood help transport oxygen, carbon dioxide, iron
nutrients and gases and lipids.

• Key examples are outlined in more detail.

• Although a key example spider silk is not mentioned above as the table refers to uses within the
organism
 2.4.U7 Living organisms synthesize many different proteins with a wide range of functions.

Usage of proteins Nothing can compare with the versatility of

proteins. Their functionality and usage in
Function Description
organisms is unrivalled. Key examples
Membrane proteins cause adjacent animal cells to stick to each
Cell adhesion
other within tissues.
Membrane proteins are used for facilitated diffusion and active
Membrane
transport, and also for electron transport during cell respiration
transport
and photosynthesis.
Some such as insulin, FSH and LH are proteins, but hormones are
Hormones Insulin
chemically very diverse.
Binding sites in membranes and cytoplasm for hormones,
Receptors neurotransmitters, tastes and smells, and also receptors for light rhodopsin
in the eye and in plants.
Histones are associated with DNA in eukaryotes and help
Packing of DNA
chromosomes to condense during mitosis.
This is the most diverse group of proteins, as cells can make
Immunity immunoglobulins
huge numbers of different antibodies.
Biotechnologically has allowed us to use proteins in industry examples are:
• enzymes for removing stains in clothing detergent
• monoclonal antibodies for pregnancy tests
• insulin for treating diabetics Genetically modified organisms are often used as to produce
• Disease treatments proteins. This however is still a technically difficult and
expensive process.
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein
functions.

• Different types of silk with different functions

spider silk • Dragline silk is stronger than steel and tougher
than Kevlar
• When first made it contains regions where the
polypeptide forms parallel arrays (bottom)
• Some regions seem like a disordered tangle
(middle)
• When the stretched the polypeptide gradually
extends, making the silk extensible and very
resistant to breaking.

https://en.wikipedia.org/wiki/Spider_silk#mediaviewer/File:Araneus_diadematus_underside_1.jpg
https://en.wikipedia.org/wiki/Spider_silk#mediaviewer/File:Structure_of_spider_silk_thread_Modified.svg
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the
range of protein functions.

collagen

• A number of different forms

• All are rope-like proteins made of three
polypeptides wound together.
• About a quarter of all protein in the human body
is collagen
• Forms a mesh of fibres in skin and in blood
vessel walls that resists tearing.
• Gives strength to tendons, ligaments, skin and
blood vessel walls.
• Forms part of teeth and bones, helps to prevent
cracks and fractures to bones and teeth

https://en.wikipedia.org/wiki/Tooth_(human)#mediaviewer/File:Teeth_by_David_Shankbone.jpg
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2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the
range of protein functions.

• A hormone – signals many cells (e.g. liver cells) to

Insuli absorb glucose and help reduce the glucose
concentration of the blood.
•
n Affected cells have receptor (proteins) on their
surface to which insulin can (reversibly) bind to.
• Secreted by β cells in the pancreas and transported
by the blood.

The pancreas of type I diabetics don’t produce

sufficient insulin therefore they must periodically
inject synthetically produced insulin to correct their
blood sugar concentration.
https://en.wikipedia.org/wiki/File:Inzul%C3%ADn.jpg
http://www.biotopics.co.uk/as/insulinproteinstructure.html
 2.4.A2 Denaturation of proteins by heat or by deviation of pH from the optimum.

Denaturation of proteins
The three-dimensional conformation of proteins is stabilized by bonds or interactions
between R groups of amino acids within the molecule. Most of these bonds and
interactions are relatively weak and they can be disrupted or broken. This results in a
change to the conformation of the protein, which is called denaturation.

A denatured protein does not normally return to

its former structure – the denaturation is
Heat can
permanent. Soluble proteins often become
cause
insoluble and form a precipitate.
denaturation
: vibrations Extremes of pH can cause
within the denaturation: charges on R groups are
changed, breaking ionic bonds within
molecule the protein or causing new ionic
breaks bonds to form.
intramolecu
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