Expedience of Protein Folding Modeling during Progressive Elongation of Polypeptide Chain

ABSTRACT

The problem of protein folding, i.e. how does a polypeptide chain fold to native protein following its synthesis on the ribosome, is recognized as a major unsolved problem of biology at molecular level. To solve the problem experimental studies of denaturation and renaturation of native proteins and a variety of theoretical-computational simulations of full-length polypeptide chains have usually been used as relevant in vitro models. However, at present these conventional approaches evidently seem to be hypothetical and have been hardly found. Nevertheless, there are a lot of convincing evidences that proteins fold progressively 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 the proteins will be expedient. These points are briefly highlighted in the current minireview.