Hjälpproteiner

Hjälpproteiner, often referred to as chaperone proteins or simply chaperones, are a diverse group of proteins found in all cells of living organisms. Their primary function is to assist other proteins in achieving and maintaining their correct three-dimensional structures, a process known as protein folding. This assistance is crucial for the proper functioning of cellular machinery, as misfolded proteins can become inactive, aggregate, and lead to cellular dysfunction or disease.

Chaperones do not typically form part of the final functional structure of the proteins they assist. Instead, they bind to unfolded or partially folded polypeptides, preventing them from aggregating incorrectly or from misfolding. They can facilitate the correct folding pathway by providing a protected environment or by using energy, often in the form of ATP, to help proteins reach their native state. Some chaperones also play roles in protein translocation across membranes, protein degradation pathways for irreparably damaged proteins, and the assembly and disassembly of protein complexes. The study of hjälpproteiner is important for understanding fundamental cellular processes and has implications for the development of treatments for diseases associated with protein misfolding, such as Alzheimer's and Parkinson's.