In vitro, computational, and theoretical studies of protein folding have converged to paint a
rich and complex energy landscape. This landscape is sensitively modulated by …

Understanding how monomeric proteins fold under in vitro conditions is crucial to describing
their functions in the cellular context. Significant advances in theory and experiments have …

Protein folding should be complex. Proteins organize themselves into specific three-
dimensional structures, through a myriad of conformational changes. The classical view of …

In recent years, improvements in experimental techniques and enhancements in computing
power have revolutionized our understanding of the mechanisms of protein folding. By …

The description of protein folding pathways and the principles that govern them has proven
to be one of the most difficult problems to be solved in structural biology. But the combination …

For many decades, protein folding experimentalists have worked with no information about
the time scales of relevant protein folding motions and without methods for estimating the …

I revisit the Levinthal paradox of protein folding kinetics. Efficient computational methods are
now finding or approaching native states on model free energy landscapes for small …

An intriguing feature of protein folding is that the overall behavior obeys simple physical
rules, but the finer details show a great deal of complexity. The scaling of thermodynamic …

Advances in simulation techniques and computing hardware have created a substantial
overlap between the timescales accessible to atomic-level simulations and those on which …

This Perspective highlights studies of protein structure, stability, and folding kinetics that can
now be carried out in prokaryotic and eukaryotic cells. The general features of cooperative …