Proteins

3.
Proteins
Proteins are large, complex molecules that
are critical for the normal functioning of the
human body.
 FUNCTIONS:
1. Enzyme catalysis: facilitate biochemical reactions
✘ Enzyme: Proteases- Break down proteins
2. Defense
✘ Immunoglobulin: Antibodies- Mark foreign proteins for elimination
and involved in defending the body from antigens
3.Transport
✘ Membrane transporters: Sodium–potassium pump: Excitable
membranes
4. Support
✘ Fibers: Collagen- Forms cartilage
 FUNCTIONS:
5. Motion
✘ Muscle: Actin- Contraction of muscle fibers
✘ contractile proteins
6. Regulation
✘ Osmotic proteins: Serum albumin- Maintains osmotic
concentration of blood
✘ Hormones: Insulin- Controls blood glucose levels
7. Storage
✘ Ion-binding: Ferritin Stores iron, especially in spleen
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein
functions.

• Full name ribulose bisphosphate carboxylase

Rubisco • Enzyme - catalyses the reaction that fixes
carbon dioxide from the atmosphere
• Provides the source of carbon from which all
carbon compounds, required by living
organisms, are produced.
• Found in high concentrations in leaves and
algal cells

http://upload.wikimedia.org/wikipedia/commons/b/b0/Mint-leaves-2007.jpg
http://upload.wikimedia.org/wikipedia/commons/thumb/7/74/Rubisco.png/220px-
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

Insulin cells) to absorb glucose and help reduce the
glucose concentration of the blood.
• 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.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein
functions.

immunoglobulins

• Also known as antibodies.

• Two antigen (a molecule on the pathogen which provokes an
immune response) binding sites - one on each ‘arm’
• Binding sites vary greatly between immunoglobulins
(hypervariable) to enable them to respond a huge range of
pathogens.
• Other parts of the immunoglobulin molecule cause a response,
e.g. acting as a marker to phagocytes (which engulf the
pathogen) https://upload.wikimedia.org/wikipedia/commons/thumb/a/a9/Antibody_IgG2.png/320px-Antibody_IgG2.png
 2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein
functions.

rhodopsin

• A pigment that absorbs light

• Membrane protein of rod cells of the retina (light sensitive region
at the back of the eye)
• Rhodopsin consists of the opsin polypeptide surrounding a retinal
prosthetic group
• retinal molecule absorbs a single photon of light -> changes
shape -> change to the opsin -> the rod cell sends a nerve
impulse to the brain
• Even very low light intensities can be detected.
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
http://chempolymerproject.wikispaces.com/file/view/collagen_%28alpha_chain%29.jpg/34235269/collagen_%28alpha_chai
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

spider silk •
functions
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
AMINO ACID
Monomer of Proteins
✘contain an amino group (—NH2) and an
acidic carboxyl group (—COOH).
There are 20 different amino acids in polypeptides synthesized
on ribosomes.

There are 22 amino acids, but only

20 amino acids are encoded by the
universal genetic code.
The Anatomy of an Amino Acid

Figure 6.2b
• Amino acids are linked together by condensation to form
polypeptides.

A ribosome condenses two amino

acids into a dipeptide forming a
peptide bond

The bonds formed are

types of covalent bonds.

Bonding monomers
together creates a
polymer (mono = one,
poly = many)
 “OMG I HAVE TO LEARN
THE NAMES OF ALL 20 !?!?”

“Relax, no you don’t, you just

need an awareness of the
concepts as outlined.”
 Different levels of protein structure

✘The four levels of

protein structure
are:
✘primary structure,
✘secondary
structure,
✘ tertiary structure,
✘quaternary
structure.
 native conformation: shape into which a protein
naturally folds
Primary structure : refers to the linear sequence of
amino acids joined to each other through peptide bonds.
 secondary protein structures: describes a regular
repeating local structure stabilized by hydrogen bonds

• peptide
groups could
interact with
one another.
• the peptide
was coiled into
a spiral α helix
secondary protein structures

✘occur between
regions of peptide
aligned next to each
other to form a planar
structure
β-pleated sheet
 TERTIARY STRUCTURE

✘When several
secondary structures
come together,
tertiary structures
are formed.
✘controls the basic
function of a protein
quaternary protein structures

✘When several tertiary

structures come
together, a quaternary
protein structure is
formed.
quaternary protein structures

✘hemoglobin is a
functional
quaternary protein
formed by the
coming together of
four tertiary
structures, called
globin proteins.