Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like
conformations. Additionally, they can fold into well-defined three-dimensional structures or …

Collapse of unfolded protein chains is an early event in folding. It affects structural properties
of intrinsically disordered proteins, which take a considerable fraction of the human …

Unfolded proteins under strongly denaturing conditions are highly expanded. However,
when the conditions are more close to native, an unfolded protein may collapse to a …

The early events in protein collapse and folding are guided by the protein's elasticity. The
contributions of entropic coiling and poor solvent effects like hydrophobic forces to the …

The application of hydrostatic pressure generally leads to protein unfolding, implying, in
accordance with Le Chatelier's principle, that the unfolded state has a smaller molar volume …

Under physiological conditions, a protein undergoes a spontaneous disorder⇌ order
transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its …

Dissecting a protein unfolding process into individual steps can provide valuable information
on the forces that maintain the integrity of the folded structure. Solvation of the protein core …

Protein stability often is studied in vitro through the use of urea and guanidinium chloride,
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …

Polypeptide chain collapse is an integral component of a protein folding reaction. In this
review, experimental characterization of the interplay of polypeptide chain collapse …

Despite the growing application of gas-phase measurements in structural biology and drug
discovery, the factors that govern protein stabilities and structures in a solvent-free …