Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

Theory and simulations predict that the structural concert of protein folding reactions is
relatively low. Experimentally, folding cooperativity has been difficult to study, but in recent …

Differential scanning calorimetry (DSC) is a very powerful tool for investigating protein
folding and stability because its experimental output reflects the energetics of all …

Protein unfolding thermodynamic parameters are conventionally extracted from equilibrium
thermal and chemical denaturation experiments. Despite decades of work, the degree of …

Transition between conformational states in proteins is being recognized as a possible key
factor of function. In support of this, hidden dynamic NMR structures were detected in several …

Despite the recent advances in the prediction of protein structures by deep neutral networks,
the elucidation of protein-folding mechanisms remains challenging. A promising theory for …

Statistical mechanical models that afford an intermediate resolution between macroscopic
chemical models and all-atom simulations have been successful in capturing folding …

Conspectus The function of proteins as biological nanomachines relies on their ability to fold
into complex 3D structures, bind selectively to partners, and undergo conformational …

The chemical shifts of backbone amide protons in proteins are sensitive reporters of local
structural stability and conformational heterogeneity, which can be determined from their …

Elucidating the protein folding mechanism is crucial to understand how proteins acquire
their unique structures to realize various biological functions. With this aim, the …