Determinants of Tertiary Structure
In globular proteins, tertiary interactions are frequently stabilized by the sequestration of hydrophobic amino acid residues in the protein core, from which water is excluded, and by the consequent enrichment of charged or hydrophilic residues on the protein's water-exposed surface. In secreted proteins that do not spend time in the cytoplasm, disulfide bonds between cysteine residues help to maintain the protein's tertiary structure. A variety of common and stable tertiary structures appear in a large number of proteins that are unrelated in both function and evolution - for example, many proteins are shaped like a TIM barrel, named for the enzyme triosephosphateisomerase. Another common structure is a highly stable dimeric coiled coil structure composed of 2-7 alpha helices. Proteins are classified by the folds they represent in databases like SCOP and CATH.
Read more about this topic: Protein Tertiary Structure
Famous quotes containing the words tertiary and/or structure:
“Morality is a venereal disease. Its primary stage is called virtue; its secondary stage, boredom; its tertiary stage, syphilis.”
—Karl Kraus (1874–1936)
“Agnosticism is a perfectly respectable and tenable philosophical position; it is not dogmatic and makes no pronouncements about the ultimate truths of the universe. It remains open to evidence and persuasion; lacking faith, it nevertheless does not deride faith. Atheism, on the other hand, is as unyielding and dogmatic about religious belief as true believers are about heathens. It tries to use reason to demolish a structure that is not built upon reason.”
—Sydney J. Harris (1917–1986)