BIOLOGY

PROTEINS
BY:
MAZNI HAMIEZAH BINTI MAHADIR ZAI NORFARIZ BIN AB MALIK FERRA ARDILLA BINTI FAUZI

SECONDARY

TERTIARY

PRIMARY

WHAT IS THE FOUR LEVELS OF PROTEIN?

QUATERNARY

Quaternary level

Tertiary level

Looks like 3D due to protein folding

2 or more tertiary level combined to form a single protein

Secondary level

-helix and -pleated sheets

Primary level

Basic order of amino acid

Primary Level

composed of amino acid linked together linearly in 1 termed peptides bond The order of the amino acids occur is specific for each polypeptides.

Secondary Level

Repeated regular structure of protein structure bind to 1 hydrogen bonding Alpha helix similar to a DNA chromosomes Beta-pleated sheets similar to corrugation of cardboards

Tertiary Level

It is the complex, 2. three-dimensional protein shape resulting 3. from the folding of the polypeptide due to 4. different types of bonds between the amino acids. Shape is maintained by intermolecular bond:- 1. Van der Waal force

H bond between NH & COO group Disulphide bridge/ bond between SH-SH Ionic bond, NH & COO These bonds include hydrogen bonds, and disulphide linkages Example : enzymes (2nd + 2nd )or (2nd + 1st )

Quaternary Level

The most complicated bonded together form of a protein. Another level is It encompasses the prosthetic group primary, secondary and e.g.: heme group in tertiary, and then adds haemoglobin (involves Fe) another level The quaternary is one or more peptide chains

Differences between fibrous & globular proteins

FIBROUS PROTEIN
Composed of many polypeptide chains, in a long narrow shape. Usually insoluble in water. eg. Collagen, which plays a structural role in the connective tissue and Actin, major component of human muscle and involved in contraction.

GLOBULAR PROTEIN
Three-dimensional shape. Mostly water soluble. eg. Haemoglobin which delivers oxygen to body tissues and hormone insulin, involved in regulating blood glucose level in humans.

Globular protein

Polar & non-polar amino acids

Amino acid s are grouped according to the properties of the side chains (R groups). Amino acids with non-polar side chains are hydrophobic, which are found in the region of proteins that are linked to the hydrophobic area of cell membrane.

Polar amino acids have hydrophilic properties and found in regions of proteins that are exposed to water.

Importance of polar & non-polar amino acids

In determining the specificity of an enzyme. Each enzyme has a region called the active site. Only specific substrate can combine with particular active sites. Combination is possible when fitting occurs. The fitting involves the general shapes and polar properties of the substrate and of the amino acids exposed at the active site.