The α-helices usually contain “cavities” (i.e., empty spaces) at the center (“core”).

The α-helices usually contain “cavities” (i.e., empty spaces) at the center (“core”).

Collagen is comprised of three “left-handed” α-helical structures.

If four monomeric units of myoglobin could interact to form a tetrameric protein, but the individual monomers would not “communicate” with each other, what would be the most likely binding profile of oxygen to the (hypothetical) tetrameric myoglobin?

Hydroxyproline is present in one of the following fibrillar proteins:

Domains are independently folded tertiary structural elements of proteins, which often possess specific functions.

In the α2β2 oligomeric structure of hemoglobin, a single αβ unit is known as:

In primary structures of proteins, amide bonds are also known as peptide bonds.

Silk fibroin is comprised of:

The binding of oxygen to hemoglobin results in changes: