GLOBULAR

PROTEIN
GROUP 1
Globular proteins usually have a
spherical shape caused by tightly
folded polypeptide chain.

• The chains are usually folded so that

hydrophobic groups are on the inside, while the
hydrophilic groups are on the outside. This
makes many globular proteins soluble in water.
GLOBULAR PROTEINS

• Varied sequence of amino acids

• They have very specific shapes which allows them to
carry out very specific function.
• Non-polar hydrophobic R groups (center/inside)
• Hydrophilic, polar R groups (surface/outside)
• Globular proteins have metabolic functions
FUNCTIONS OF GLOBULAR PROTEIN
• TRANSPORT PROTEIN
– HEMOGLOBIN
– MYOGLOBIN
• HORMONES
– INSULIN
– ESTROGEN
• ENZYMES
– PEPSIN
– LIPASE
HEMOGLOBIN
- OXYGEN TRANSPORT FUNCTION
• 4 polypeptide chains
• 2 α and 2 β chains
• nearly spherical in shape
• Hydrophobic R groups point inward. Important to maintain the
3D shape.
• Hydrophilic R groups point outwards. Important to maintain its
solubility.
• Each polypeptide contains a prosthetic group called heme group.
• Heme group contains iron ion Fe2+
HEMOGLOBIN
 HEMOGLOBIN FUNCTION
• Carries oxygen from the lungs to
tissues
– A Hb molecule contains 4 heme
groups and carries 4 molecules of
O2
• Carries carbon dioxide from tissues
back to the lungs
TYPES OF HEMOGLOBIN
• Fetal hemoglobin (HbF)- Major hemoglobin found in the fetus and newborn
• HbA2 -Appears -12 weeks after birth
• HbA1c - HbA1c levels are high in patients with diabetes mellitus

HEMOGLOBINOPATHIES
• Sickle cell (HbS) disease
– Caused by a single mutation in b-globin gene
• Hemoglobin C disease
– Caused by a single mutation in b-globin gene
MYOGLOBIN
-STORES AND SUPPLIES OXYGEN TO THE HEART AND MUSCLE ONLY

• Single polypeptide chain forming a single subunit with eight a-helix

structures.
• The interior of the subunit is composed of nonpolar amino acids
• The charged amino acids are located on the surface
• With one prosthetic group (heme) which is present at the center of the
molecule
• Binds only with oxygen and supplies oxygen to the muscles only.
• Myoglobin gives red color to skeletal muscles
• Supplies oxygen during aerobic exercise
INSULIN
- M A I NT AI NS B LOO D G L UCOS E C ONCE NT R A T I ON.

• Hormone insulin is made and secreted by the pancreas.

• 2 Polypeptide chains (α-helix & β-pleaded sheet)
• Joined together by Disulphide links.
• The shape of insulin allows it to specifically bind to
receptors on cell membranes to help lower blood glucose
concentration.
• Insulin also has hydrophilic R groups on the outside
making it soluble in water. This allows insulin to dissolve
in the blood and be easily transported around the body.
 INSULIN FUNCTION
• helps control blood glucose
levels by signaling the liver
and muscle and fat cells to
take in glucose from the
blood.
• helps cells to take in
glucose to be used for
energy. If the body has
sufficient
energy, insulin signals the
liver to take up glucose and
store it as glycogen.
PEPSIN
- BREAKS DOWN LARGE PROTEINS INTO SMALLER PEPTIDES
• Found in the stomach which is an acidic environment (low pH)
• Becomes denatured at low pH because they contain amino acids with basic
(base) R groups.
• Basic R groups accept hydrogen ions and become positively charged.
• Positively charged R groups can affect the ionic bonds an hydrogen bonds in
the protein– this denatures the enzyme and therefore alters its function.
• The primary structure of pepsin has very few basic R groups, preventing the
tertiary structure from being affected by the low pH.
• The tertiary structure of pepsin is also kept stable in shape by hydrogen bonds
and disulphide links
PEPSIN FUNCTION

• Pepsin acts on the complex dietary protein and breaks up into peptides and
amino acids which can be easily absorbed by the intestinal linings
DENATURING PROTEINS
• If the bonds that maintain a protein’s shape are broken, the protein
will stop working properly and is denatured.

• Changes in temperature, pH or salt concentration can all denature a

protein, although the specific conditions will vary from protein to
protein.