Primary Structure

The very basic strand of amino acids. Primary structure is a term that refers to the linear sequence of amino acids that make up the protein.

Secondary structure
of amino acids are linked by hydrogen bonds. This level of structure takes the form of either a pleated sheet or a helix.

Occurs when the sequence

alpha helix (-helix) is a right-

handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid.

sheet (-pleated sheet) is the

second form of regular secondary structure in proteins, only somewhat less common than the alpha helix. Beta sheets consist of beta strands connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.

Tertiary structure
The folding and other contortions of a polypeptide chain that result from the molecular interactions among the R groups of the different amino acids.

Quaternary structure
refers to the number and arrangement of the individual polypeptide chains. Each polypeptide is referred to as a subunit of the protein. The same forces and bonds that create tertiary structure also hold subunits together in a stable complex to form the complete protein.

What holds all this different protein structures together

Primary protein structure Peptide bonds Secondary protein structure Hydrogen bonds Tertiary protein structure and Quaternary protein structure Hydrogen bonds ionic bonds van der Waals interactions disulfide bridges

Denaturation
The proteins that is unfold called DENATURATION.

Denaturation refers to any change in the secondary, tertiary and quaternary levels of protein structure without cleaving the peptide bonds. This means disruption of all levels of protein structure except at the primary level.