Structures of Proteins

- Group 5

4 Types of Structures

Primary Secondary Tertiary Quaternary

Primary Structure
This is a long sequence of amino acid residues combined together forming a polypeptide chain. Each amino acid is identified by its specific R group therefore gives a number of 20 different amino acids in living things. As the result there is an incredible diversity of primary structures of protein.

Secondary Structure
This is the structure developed when the primary structure of a polypeptide has group projecting from the N-C-C backbone. The parts of the polypeptide chain take up a particular shape; either folded ( sheets) or coiled ( helix).

Tertiary Structure
This is when the molecule is further folded and held in a

particular complex shape

forming precise and compact structure, unique to that protein. The shape is maintained permanently by

the intra- molecular bonds:

Tertiary Structure

Hydrogen bond - bond of one
hydrogen atom shared by two

other atoms

Van der Waals force - the

weak force that incurs when

two or more atoms are very

close

Tertiary Structure

Disulphide bond
a strong covalent bond formed between two adjacent cysteine

amino acids. The bond

stabilizes the tertiary shape of a protein

Ionic bond
the electrostatic interaction between oppositely charged ions

Quaternary Structure
A structure of protein arise when a number of tertiary polypeptides joined together forming a complex, biologically active molecule.

Structures of Protein

Differeces Between Fibrous and Globular Proteins

Differentiate
Fibrous Proteins Shapes Tertiary structure that is long Narrow muchcoiled chain Water insoluble Collagen Keratin Globular Proteins Tertiary structure that is spherical Round shape Near soluble (colloids) Enzymes Hemoglobin Insulin

Solubility Examples

Differentiate
Fibrous Proteins Structure Collagen exists as a "triple helix". These strands usually come together to form very strong structures that resists "where-andtear". Globular Proteins They are associated with functions of transporting or act as antibodies due to their solubility.

Polar and Non-Polar Amino Acids

Amino acids containing non-polar R group would be hydrophobic, which are found in the center of water soluble proteins. Amino acids containing non-polar R group would be

hydrophobic which are found at the surface.

Polar and Non-Polar Amino Acids

How does Polar and non-Polar amino acids affect the bonding and structure of Proteins? The hydrophilic and hydrophobic properties of amino acids cause proteins to twist into useful shapes important for cellular membrane. Membrane proteins contain two polar ends and a non-polar centre that stabilise them in the phospholipid bilayer. One end contacts the extracellular fluid and the other end extends to the cytoplasm whilst the hydrophobic centre remain inside the membrane. The polarity of R groups affects the tertiary structure and shaping of globular proteins which are normally enzymes and their active sites.

Functions Structure and support Transport

Examples Collagens strengthens bones, skin and tendons Hemoglobin molecules transport oxygen to respiring tissues

Defence against disease

Immunoglobulins are antibody proteins that response to antigens that may invade body

Muscle movement

Myosin found in muscle fibre causes contraction of the muscle which results in movement

Biological catalysts

Examples of globular proteins are enzymes that alter the speed of chemical reactions in living organisms

Chemical messengers

Some hormones such as insulin secreted from the pancreas

are form of globular proteins