> The spontaneous folding of small, single-domain globular proteins, such as villin headpiece subdomain HP35, occurs on the microsecond timescale via a stochastic diffusion-collision mechanism along a rugged free energy landscape governed by the interplay of enthalpic contributions from intramolecular hydrogen bonding, van der Waals packing interactions, and hydrophobic collapse, counterbalanced by entropic penalties associated with conformational restriction, all of which are modulated by solvent-accessible surface area and mediated through solvent reorganization dynamics; this process can be quantitatively modeled using all-atom molecular dynamics simulations with explicit solvent (e.g., TIP3P water model) under the CHARMM36m force field, and validated experimentally through time-resolved Förster resonance energy transfer (FRET) and φ-value analysis, revealing folding transition states that exhibit partial secondary structure.

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