Natural protein molecules are exceptional polymers. Encoded in apparently random strings
of amino-acids, these objects perform clear physical tasks that are rare to find by simple …

Highlights•Protein sequences have evolved to function and to fold.•Residues evolved for
function cannot always be optimal for folding.•They affect folding routes, rates, kinetic …

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

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 …

Thermosensing is critical for the expression of virulence genes in pathogenic bacteria that
infect warm-blooded hosts. Proteins of the Hha-family, conserved among …

How many structurally different microscopic routes are accessible to a protein molecule
while folding? This has been a challenging question to address experimentally as single …

The aim of this study is to investigate the folding reaction of human frataxin, whose
deficiency causes the neurodegenerative disease Friedreich's Ataxia (FRDA). The …

Many intrinsically disordered proteins switch between unfolded and folded-like forms in the
presence of their binding partner. The possibility of a pre-equilibrium between the two …

We show that the phosphorylation of 4E-BP2 acts as a triggering event to shape its folding-
function landscape that is delicately balanced between conflicting favorable energetics and …