You are on page 1of 24

EPF 4602



• Protein
molecule consisting of one or more
chains of amino acids.

examples include alpha helices and pleated sheets • stabilized by hydrogen bonding TERTIARY STRUCTURE • three-dimensional structure of a protein • have a large number of non-covalent interactions between amino acids. QUARTENARY STRUCTURE • bind multiple polypeptides into a single. larger protein • Hemoglobin has quaternary structure due to association of two alpha globin and two beta globin polyproteins. SECONDARY STRUCTURE • folding or coiling within a protein. .STRUCTURE OF PROTEIN LINEAR STRUCTURE • linear arrangement of amino acids • Linked by covalent linkages such as disulfide bonds between amino acids.



haemoglobin in blood (prosthetic group. .Simple proteins Conjugated proteins • chains of amino acid units • only joined by peptide linkages. tissue globulin. iron pigment). • The non-protein material is called prosthetic group or cofactor • Examples are Mucin in saliva (prosthetic group. serum globulins. • composed of simple proteins and non protein material. glutenin in wheat. coryzenin in rice. phosphoric acid). etc. casein in milk (prosthetic group. • Examples are : Egg albumin. carbohydrate). etc.

Simple Protein .

Conjugated Protein .

myosin (muscles). pepsin. wool. Globular proteins • • • • • Fibrous proteins have more or less spherical shape (compact structure) a-helics are tightly held up by weak attractive forces of various types: Hydrogen bonding. cytochromes. salt or ionic bridges. disulphide bridges. albumins. usually soluble in water. etc. .• • • • made up of polypeptide chains that run parallel to the axis held together by strong hydrogen and disulphide bonds can be stretched and contracted like a thread usually insoluble in water. collagen (tendons. Examples are : a-keratin (hair. haemoglobin. silk and nails). Examples are: Insulin. etc. bones).



• A small protein consists of about 50 amino acids while larger proteins may contain 3.SIZE AND SHAPE • Size of protein usually measured in molecular weight (mass). gel filtration. • It can be estimated by methods including electrophoresis. and more recently by mass spectrometry. • Molecular weight of protein is the mass of one mole of protein usually measured in units daltons.000 . • Most proteins have a mass between 10 and 100 kilodaltons (kD).

. • In aqueous solutions. proteins tend to fold so that areas of the protein with hydrophobic regions are located in internal surfaces next to each other and away from the polar water molecules of the solution.HYDROPHOBICITY • Hydrophobic means fear of water.

• Polar groups on the amino acid are called hydrophilic (water loving) because they will form hydrogen bonds with water molecules. . type and distribution of nonpolar amino acid residues within the protein determines its hydrophobic character. • The number.

• For example: Cytoplasmic proteins have mostly hydrophilic (polar) amino acids on their surface and are therefore water soluble. • The 3-D structure of a protein affects its solubility properties. with more hydrophobic groups located on the interior of the protein. .SOLUBILITY • Solubility is the amount of a solute that can be dissolved in a solvent. sheltered from the aqueous environment.

proteins that reside in the lipid environment of the cell membrane have mostly hydrophobic amino acids (non polar) on their exterior surface and are not readily soluble in aqueous solutions. solvent type. • Any changes to condition such as buffer. pH. ionic strength and temperature will cause protein to lose the solubility.• In contrast. .

.ISOELECTRIC POINT • The isoelectric point (pI) of a protein is the pH where the net charge on the protein is zero. • Proteins have different isoelectric points because of their different amino acid sequences. • They can be separated by adjusting the pH of a solution.


. .Mayonnaise contains oil and water. • Emulsifiers .Give shape and structure to food.Emulsions in food are mixtures of oil and water.FOOD INDUSTRY • Gelling agent . The emulsifier keeps these mixed and without it the oil and water separate.

• Thickeners .• Foaming agent .Material that facilitates formation of foam.Thickening agents make foods thicker. .

geometrically precise intermolecular contacts is required for lattice stability. .CRYSTALIZATION • To form a high-quality crystal. a protein must be immobilized in a lattice in a consistent conformation with limited dynamic motion. • Protein surface properties play a determining role in controlling crystallization behavior because formation of tight.

• Elastin will serve as a scaffold which can be sewed or glued in the place of a missing part. • It will hold the artery or organ closed and intact while at the same time it can also be populated by the body's own cells .FABRIC FROM ELASTIN • Elastin is a matrix protein. • It gives skin and blood vessels their elasticity. It holds the cells together into tissues and provides natural support and flexibility.

• The blends were processed by compounding extrusion and injection molding. .SOY PROTEIN-BASED PLASTICS • Blending soy protein with polyesters using a polyvinyllactam as a compatibilizer successfully made soy protein-based plastics. • Blends made from soy protein flour produced plastics with the lowest water absorption.

Thank you .