Although protein folding is a simple outcome of the underlying thermodynamics, arriving at a
quantitative and predictive understanding of how proteins fold nevertheless poses huge …

PACE, a hybrid force field that couples united-atom protein models with coarse-grained (CG)
solvent (J. Chem. Theory Comput. 2010, 6, 3373), has been further optimized, aiming to …

Non‐equilibrium molecular dynamics simulations of a solvated 21‐residue polyalanine
(A21) peptide, featuring a high propensity for helix formation, have been performed at 300 K …

Simple helix–coil transition theories have been indispensable tools in the analysis of data
reporting on the reversible folding of α-helical polypeptides. They provide a transferable …

The rate-limiting step in the formation of the native dimeric state of human Cu, Zn superoxide
dismutase (SOD1) is a very slow monomer folding reaction that governs the lifetime of its …

While both turn formation and hydrophobic interactions play dominant roles in the initiation
of protein folding, their individual contributions to the folding kinetics and to the structural …

The information obtained by studying fluorescence decay of labeled biopolymers is a major
resource for understanding the dynamics of their conformations and interactions. The …

We utilize T-jump UV resonance Raman spectroscopy (UVRR) to study the impact of ion
binding on the equilibrium energy landscape and on (un) folding kinetics of poly-l-lysine …

We review our joint experimental-theoretical effort on the folding of photo-switchable α-
helices. The folding kinetics of these peptides is profoundly non-exponential, which is …