THE FOLDING PROCESS OF HEN LYSOZYME - A PERSPECTIVE FROM THE NEW VIEW

How a conformationally disordered polypeptide chain rapidly and effici ently achieves its well-defined native structure is still a major ques tion in modern structural biology. Although much progress has been mad e towards rationalizing the principles of protein structure and dynami cs, the mechanism of the folding process and the determinants of the f inal fold are not yet known in any detail. One protein for which foldi ng has been studied in great detail by a combination of diverse techni ques is hen lysozyme. In this article we review the present state of o ur knowledge of the folding process of this enzyme and focus in partic ular on recent experiments to probe some of its specific features. The se results are then discussed in the context of the 'new view of prote in folding based on energy surfaces and landscapes. It is shown that a schematic energy surface for lysozyme folding, which is broadly consi stent with our experimental data, begins to provide a unified model fo r protein folding through which experimental and theoretical ideas can be brought together.