Abstrait

Protein folding: Requirement for simulations on the basis of sequential growth of polypeptides

Mahmud A.Basharov

To solve the problemof protein folding, denaturation-renaturation experiments on native proteins and a variety of theoretical-computational simulations of full-length polypeptide chains have usually been used as convenient in vitro models for the past several decades. However, there is a lot of irrefutable evidence that the information contained in the primary structure of a protein about its spatial structure is realized in the cells during the residue-by-residue elongation on the ribosome from the N- to the C-terminus. On this basis therefore, simulations of the folding and formation of the native spatial structure of proteinswill be of requirement.