The characterization of protein-folding kinetics with increasing chain length under various thermodynamic conditions is addressed using the capillarity picture in which distinct spatial regions of the protein are imagined to be folded or trapped and separated by interfaces. The quantitative capillarity theory is based on the nucleation theory of first-order transitions and the droplet analysis of glasses and random magnets. The concepts of folding funnels and rugged energy landscapes are shown to be applicable in the large size limit just as for smaller proteins. An ideal asymptotic free-energy profile as a function of a reaction coordinate measuring progress down the funnel is shown to be quite broad. This renders traditional transition state theory generally inapplicable but allows a diffusive picture with a transition-state region to be used. The analysis unifies several scaling arguments proposed earlier. The importance of fluctuational fine structure both to the free-energy profile and to the glassy dynamics is highlighted. The fluctuation effects lead to a very broad trapping-time distribution. Considerations necessary for understanding the crossover between the mean field and capillarity pictures of the energy landscapes are discussed. A variety of mechanisms that may roughen the interfaces and may lead to a complex structure of the transition-state ensemble are proposed.