Fibrous and globular

proteins
AS Bio
Globular proteins
• A globular protein is a protein whose molecules are folded into a relatively
spherical shape and compact in shape
• Globular proteins are generally water-soluble and have physiological roles
• Globular proteins form a spherical shape when folding into their tertiary
structure because:
• their non-polar hydrophobic R groups are orientated towards the centre of the protein
away from the aqueous surroundings
• their polar hydrophilic R groups orientate themselves on the outside of the protein
• This orientation enables globular proteins to be (generally) soluble in water as
the water molecules can surround the polar hydrophilic R groups
• The solubility of globular proteins in water plays an important physiological roles
as they can be easily transported around organisms and be involved in metabolic
reactions
Folding in globular proteins
Globular proteins
• Globular proteins have roles in metabolic reactions:
-Enzymes - catalyse metabolic reactions
- Haemoglobin - binds to oxygen to transport it around body
• Enzymes are globular proteins
• The folding of the protein due to the interactions between the R groups results in
globular proteins having specific shapes.
• This also enables globular proteins to play physiological roles, for
example, enzymes can catalyse specific reactions and immunoglobulins can
respond to specific antigens
• Some globular proteins are conjugated proteins that contain a prosthetic group
e.g. haemoglobin which contains the prosthetic group called haem
Haemoglobin
• Haemoglobin is a protein with a globular structure
• It is the oxygen-carrying pigment found in red blood cells
• Haemoglobin has a quaternary structure made up of 4 separate polypeptide chains
i.e. 2 identical alpha -chains with 141 amino acids each and 2 identical beta -chains with
146 amino acids each
• Each polypeptide chain is folded/coiled into a compact shape due to hydrophobic
interactions between the (hydrophobic) R groups
• All 4 polypeptide chains are linked to form a roughly spherical haemoglobin molecule
• The precise 3D-shape of the Haemoglobin molecule is absolutely critical to its oxygen-
carrying function
• The Hydrophilic R-groups are arranged around the outside of the molecule which
allows Haemoglobin to mix with the watery medium inside red blood cells
Haemoglobin
• Attached to each polypeptide chain is a prosthetic haem group with
an Fe2+ ion
• Each Fe2+ ion can combine with one oxygen (O2) molecule
• Human haemoglobin has four polypeptide chains and four haem
groups and can therefore carry 4 Oxygen molecules making it an
efficient respiratory pigment involved in oxygen transport
• When haemoglobin is bound to oxygen it is called oxy-haemoglobin
Haemoglobin structure
Haemoglobin structure
Fibrous proteins
• A fibrous protein is a protein which is made up of long polypeptide chains running parallel to
each other. These have cross linkages due to hydrogen bond
• The fibrous protein molecules have a relatively long, thin structure
• Fibrous proteins are generally insoluble and metabolically inactive
• Their function is usually structural
• They have little or no tertiary structure
• Due to the large number of hydrophobic R groups fibrous proteins they are insoluble in water
• Fibrous proteins have a limited number of amino acids with the sequence usually being highly
repetitive
• The highly repetitive sequence creates very organised structures that are strong and this along
with their insolubility property, makes fibrous proteins very suitable for structural roles
• For example, keratin that makes up hair, nails, horns and feathers and collagen which is a
connective tissue found in skin, tendons and ligaments
Collagen
• Collagen is an insoluble fibrous protein
• It is found in skin, tendons, cartilage, bones, teeth and the walls of blood vessels
• Collagen has three polypeptide chains wound around each other to form a triple helix. Each
chain is a lose helix not α -helix
• There are about 1000 amino acid residues in each chain
• The complete triple helix compound is tropocollagen
• The three strands are held together by hydrogen bonds and some by covalent bonds
• Hydrogen bonds are formed between –NH groups of glycine in one chain and –CO groups of
Proline in the other chain
• Many triple helix can be parallel to each other to form fibrils.
• They are joined by covalent bonds.
• Fibrils in turn unite to form fibers
Collagen
• Every third amino acid is glycine
• Glycine is small in size and found on the inside of the strands
• Allows the three strands to lie close together and form a tight coil
• Covalent bonds form between R groups of amino acids lying next to
each other
• Cross links hold collagen molecules side by side forming fibrils
Collagen
The Primary structure of collagen
• a repeat sequence of 3 amino acids glycine-proline-X (any other amino acid)
The Secondary/Tertiary Structure of Collagen
• glycine is the smallest amino acid and this together with proline allow the polypeptide
chain to be wound into a tightly coiled, straight and unbranched helix
The Quaternary Structure of Collagen
• 3 of these helical polypeptides are wound around each other and held by H-bonds.
• The triple stranded molecules run parallel to others and disulphide cross-linkages
between the R-groups of the amino acid lysine holds the molecules together forming
fibres
• The ends of the collagen molecules are staggered to avoid weak points giving collagen
¼ the tensile strength of steel
Structure to function of collagen
• Collagen is fibrous
• Consists of primary structure of repetitive tripeptide sequences that
form long chains and may run parallel to each other
• Its secondary structure has three unbranched polypeptide chains
linked to one another via cross bridges forming a triple helix
• The cross bridges provide structural support to collagen molecule
therefore making it resistant to stretching (has a high tensile strength)
• Collagen has important structural role in providing physical strength
to connective tissue such as tendons