We present an analysis of the folding behavior of the 159-residue major birch pollen
allergen Bet v 1. The protein contains a water-filled channel running through it …

The folding reactions of many small, globular proteins exhibit two-state kinetics, in which the
folded and unfolded states interconvert readily without observable intermediates. Typically …

Using mutational analysis, three groups have compared the transition states for the folding
of two pairs of homologous proteins. The results of these studies suggest that protein folding …

Apparent transition state movement upon mutation or changes in solvent conditions is
frequently observed in protein folding and is often interpreted in terms of Hammond …

Classical protein folding invokes a cooperative transition between distinct thermodynamic
states that are individually populated at equilibrium and separated by an energy barrier. It …

The genome project, with the discovery of thousands of new protein sequences every year,
has created a revolution in protein physics, chemistry, and biology. This has led to a …

Investigators have recently turned to studies of protein families to shed light on the
mechanism of protein folding. In small proteins for which detailed analysis has been …

The description of protein folding mechanisms in terms of the structures of well defined,
partially folded intermediates is a major objective in structural biology. Despite the fleeting …

We argue that folding of the compact domains of proteins can occur with adequate rapidity in
the absence of a unique directed mechanism, provided that native-like local structure …

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