After conquering the atomic structure about a century ago, chemists have been largely
interested in understanding the concept of chemical bond and the formation of a molecule …

The argument that the hydrophobic effect is the primary effect driving the folding of globular
proteins is nearly universally accepted (including by the authors). But does this view also …

All structured biological macromolecules must overcome the thermodynamic folding
problem to populate a unique functional state among a vast ensemble of unfolded and …

Small proteins with globular structures often fold by simple all-or-none mechanisms, both in
an equilibrium and a kinetic sense, despite the very large number of partly folded …

The chaperonin complex GroEL–GroES is able to accelerate the folding process of knotted
proteins considerably. However, the folding mechanism inside the chaperonin cage is …

We introduce a Firefly-inspired algorithmic approach for protein structure prediction over two
different lattice models in three-dimensional space. In particular, we consider three …

We carry out systematic Monte Carlo simulations of Gō lattice proteins to investigate and
compare the folding processes of two model proteins whose native structures differ from …

Gō models are exceedingly popular tools in computer simulations of protein folding. These
models are native-centric, ie, they are directly constructed from the protein's native structure …

The nucleation mechanism of protein folding, originally proposed by Baldwin in the early
1970s, was firstly observed by Shakhnovich and co-workers two decades later in the context …

Despite the large and complex conformational space available to an unfolded protein, many
small globular proteins fold with simple two-state cooperative kinetics. Understanding what …