Principles of Protein Folding

Protein folding is a process in which a polypeptide folds into a specific, stable, functional, three-dimensional structure. It is the process by which a protein structure assumes its functional shape or conformation. Proteins are comprised of amino acids with various types of side chains, which may be hydrophobic, hydrophilic or electrically charged. It is now well known that under physiological conditions, proteins normally spontaneously fold into their native conformations but there are some exterior factors which help polypeptide chain finding its natural shape. Different levels of folding a protein after amino acid sequence or primary structure consist of secondary, tertiary and quaternary structures. Protein folding pathway or mechanism is the typical sequence of structural changes; in which protein find its native structure. 3D structure of proteins is studied by scientists using different methods and there are many types of software to survey this. Many factors control protein folding, interior and exterior factors. Creation of natural folded proteins by these factors and protein translation are simultaneous. The main objective of this review is to unveil the fact; despite there are many factors controlling protein folding, mainspring is amino acids sequence which itself rises from chemo-physical laws.