Abstract:

It is generally accepted that one or more distinct, populated intermediates are involved in the folding of most proteins. Although the understanding of the tertiary structure of the intermediate is important to elucidate the hierarchic folding pathway, it is difficult to characterize the structure because it exists only transiently during the folding process. Recently, it has been shown that several globular proteins, when placed under certain denaturing conditions, can exist in equilibrium molten globule states.