Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure. Hence, they
are often misconceived to present a challenge to Anfinsen's dogma. However, IDPs exist as …

We developed both analytical and simulation methods to explore the diffusion dynamics in
protein folding. We found the diffusion as a quantitative measure of escape from local traps …

We show that diffusion can play an important role in protein-folding kinetics. We explicitly
calculate the diffusion coefficient of protein folding in a lattice model. We found that diffusion …

Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure but exist as
conformational ensembles. Because of their structural plasticity, they can interact with multiple …

The energy landscape approach has played a fundamental role in advancing our understanding
of protein folding. Here, we quantify protein folding energy landscapes by exploring the …

Molecular dynamics (MD) simulations have become increasingly powerful and can now
describe the folding/unfolding of small biomolecules in atomic detail. However, a major …

The amyloid-β (Aβ) monomer, an intrinsically disordered peptide, is produced by the cleavage
of the amyloid precursor protein, leading to Aβ-40 and Aβ-42 as major products. These …

Intrinsically disordered proteins (IDPs) lack a rigid three-dimensional structure and populate
a polymorphic ensemble of conformations. Because of the lack of a reference conformation, …

To reveal the molecular determinants of biological function, one seeks to characterize the
interactions that are formed in conformational and chemical transition states. In other words, …

The folding process of multidomain proteins is a highly intricate phenomenon involving the
assembly of distinct domains into a functional three-dimensional structure. During this process…