Stretches or strands of proteins have distinct characteristics local structural conformations dependent on hydrogen bonding
The secondary structure involves repeated folding of polypeptides, the building blocks of proteins. Hydrogen bonding stabilizes the structure.
There are two major types of secondary structures: alpha-helix and beta-pleated sheets
Linus Pauling first predicted that the alpha-helix exists. His prediction was confirmed by Max Perutz and John Kendrew viewed myoglobin with x-ray crystallography. They won the 1962 Nobel Prize in chemistry 1962 for this accomplishment.
Alpha-helix: This structure involves an amine group hydrogen bonded to a carbonyl group. These structures are found in skin, hair, and other fibrous proteins. An alpha-helix has 3.6 residues/ turn meaning that every 100 degrees of rotation contains a single residue. A residue is simply a monomer that is a building block for any structure, in this case a protein. Carbonyl groups face the amine groups and are four residues away from each other. This is what forms the strong hydrogen bond that gives this structure so much stability. The alpha-helix is the most important structural component of proteins. However, there are additional helix structures that are found in proteins. These different helix structures differ in the sizes of their radii compared to the alpha-helix.
Beta-pleated sheets: This structure is another major type in proteins. It is comprised of sheets that are made up of beta-strands that are connected by hydrogen bonds.