Properties
|
Fibrous Protein
|
Globular protein
|
Definition
|
A
class of insoluble protein which constitute the main structural elements of
the body.
|
A class of soluble protein and tend to be involved
in metabolic function.
|
Role
|
Involved in forming structures and mechanical function
|
Involved in metabolic reaction and chemical processes
|
Solubility in water,
acids and bases
|
Insoluble
|
Soluble
|
Sequences of amino
acids
|
Consists of repetitive sequences of amino acids
|
Consists of irregular sequences of amino acids
|
Dominated
|
Dominated by secondary structure
|
Dominated by tertiary structure
|
Shape
|
Has long and narrow shape
|
Has round and spherical shape
|
Strength of
intermolecular interaction
|
Have strong intermolecular interaction
|
Have weak intermolecular interaction
|
Structure
|
Have a helical or sheet structure
|
Have a folded ball-like structure
|
Sensitivity toward
temperature and pH
|
Less sensitive
|
More sensitive
|
Amount
|
The number of proteins is lower
|
The number of proteins is comparatively higher
|
Examples
|
|
|
TAY YU LIANG-71789
Nur Izzati Binti Jeafree-72545
|
Elongated strand-like protein
|
DEFINITION
|
Spherical protein
|
|
As strength, protection and support
|
ROLE
|
As catalyst, transport and regulation
|
|
long and narrow
|
SHAPE
|
rounded ball
|
|
Insoluble
|
SOLUBLE IN WATER
|
Soluble
|
|
Repetitive
|
SEQUENCE OF AMINO ACID
|
Irregular
|
|
Less sensitive
|
CHANGE IN HEAT AND pH
|
More sensitive
|
|
Low
|
AMOUNT OF PROTEIN
|
Comparatively higher
|
|
Stable
-many Hydrogen bond that hold the structure
|
STABILITY
|
Unstable
-easily distributed
-less bond hold together
|
|
In the secondary structure
|
SRUCTURE
|
In the tertiary structure
|
|
Strong
|
INTERMOLECULAR INTRACTION
|
Weak
|
|
Keratin, collagen, desmin, elastin fibroin, myosin
|
EXAMPLES
|
Enzymes, haemoglobin, insulin, myoglobin,
transferrin, immunoglobin, catalase, hormones
|
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