Protein folding is the process by which a polypeptide chain folds into a bioactive protein in a three-dimensional structure. During translation, each protein exists first as an unfolded polypeptide or random coil after being translated from mRNA to a linear chain of amino acids. The amino acids in the chain eventually interact with each other to form a well-defined folded protein. Hydrophobic effects, Vander Waals forces, H-bonds, and hydrostatic interactions drive the formation of complex protein structures. The amino acid sequence of a protein determines its three-dimensional structure that is critical to its function.
Protein folding is a very sensitive process that is influenced by several external factors including electric and magnetic fields, temperature, pH, chemicals, space limitation, and molecular crowding. These factors influence the ability of proteins to fold into their correct functional forms. In vivo, proteins that do not fold correctly may be unstable or inactive, or even toxic, leading to dysfunction and many diseases.
Amerigo Scientific offers a wide range of protein folding tools for properly folding proteins into active proteins from inclusion bodies.
Note: If you don't receive our verification email, do the following: