Protein Folding

 Proteins have several layers of structure each of which is vital within the process of folding. Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation which is usually biologically functional, in an expeditious and reproducible manner. Proteins are folded and held together by several sorts of molecular interactions. The molecular interactions include the thermodynamic stability of the complex, the hydrophobic interactions and thus the disulfide bonds formed within the proteins. the foremost important factor in a proteins ability to fold is that the thermodynamics of the structure. The duration of the folding process varies dramatically depending upon the protein of interest. During translation, each protein is synthesized as a linear chain of amino acids or a random coil which doesn't have a stable 3D structure. The amino acids within the chain eventually interact with one another to make a well-defined, folded protein. The amino acid sequence of a protein determines its 3D structure. Folding of proteins into their correct native structure is vital to their function. Failure to fold properly produces inactive or toxic proteins that malfunction and cause variety of diseases. Extreme temperatures affect the steadiness of proteins and cause them to unfold or denature. Similarly, extreme pH, mechanical forces and chemical denaturants can denature proteins.