Ken A. Dill and Hue Sun Chan (1997) illustrated a folding pathway design based on Levinthals Paradox, named the "golf-course" landscape, where a random searching for the native states would prove impossible, due to the hypothetically "flat playing field" since the protein "ball" would take a really long time to find a fall into the native "hole". However, a rugged pathway deviated from the initial smooth golf-course creates a directed tunnel where the denatured protein goes through to reach its native structure, and there can exist valleys (intermediate states) or hills (transition states) long the pathway to a proteins native state. Yet, this proposed pathway yields a contrast between pathway dependence versus pathway independence, or the Levinthal dichotomy and emphasizes the one-dimensional route of conformation.
Another approach to protein folding eliminates the term "pathway" and replaces with "funnels" where it is concerned with parallel processes, ensembles and multiple dimensions instead of a sequence of structures a protein has to go through. Thus, an ideal funnel consists of a smooth multi-dimensional energy landscape where increasing interchain contacts correlate with decreasing degree of freedom and ultimately achievement of native state.  
Unlike an idealized smooth funnel, a rugged funnel demonstrates kinetic traps, energy barriers, and some narrow throughway paths to native state. This also explains an accumulation of misfolded intermediates where kinetic traps prevent protein intermediates from achieving their final conformation. For those that are stuck in this trap, they would have to break away favorable contacts that do not lead to their native state before reaching their original starting point and find another different search downhill. A Moat landscape, on the other hand, illustrates the idea of a variation of routes including an obligatory kinetic trap route that protein chains take to reach their native state. This energy landscape stems from a study by Christopher Dobson and his colleagues about hen egg white lysozyme, in which half of its population undergo normal fast folding, while the other half first forms α-helices domain quickly then β-sheet one slowly. It is different from the rugged landscape since there are no accidental kinetic traps but purposeful ones required for portions of protein to go through before reaching the final state. Both the rugged landscape and the Moat landscape nonetheless present the same concept in which protein configurations might come across kinetic traps during their folding process. On the other hand, the Champagne Glass landscape involves free energy barriers due to conformational entropy that partly resembles the random golf-course pathway in which a protein chain configuration is lost and has to spend time searching for the path downhill. This situation can be applied to a conformational search of polar residues that will eventually connect two hydrophobic clusters.