Protein Archetype: The Chaperone
Yes, the cellular environment can be full of all kinds of snares for a young, not yet fully formed protein. New-come to the world, some proteins have to be chaperoned in their early life. If not, they might meet a bad end. And I’m talking a really bad end: like being whisked off and chopped up to bits. Thankfully, the strict, straight-laced chaperone proteins are present to help a new protein make something worthwhile out of itself. Broadly Speaking: In a cell, there are many proteins which function as “molecular chaperones.” Chaperone proteins are most commonly found in the cytoplasm as well as in the lumen, or inner portion, of the organelle called the endoplasmic reticulum. Chaperones in general have three main jobs to do. These jobs are: helping newly-made proteins get into the proper shape for their future careers, keeping proteins from clumping up together after a stressful event, and finally, refolding stressed-out proteins back into shape. The job description for molecul...