What creates the tertiary structure of a protein?

The tertiary structure of a protein is primarily established by interactions among the various side chains, or R groups, of the amino acids that make up the protein. These R group interactions include a variety of bonding types such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, all of which contribute to the overall 3D shape of the protein.

Understanding that the tertiary structure is a result of the overall folding and arrangement dictated by these interactions is crucial. Each R group can influence the folding of the protein in specific ways, depending on its chemical properties (e.g., hydrophobic, polar, charged), ultimately determining how the protein will function in a biological context. Thus, focusing on the bonds between different R groups captures the essence of how the tertiary structure is stabilized and shaped.