Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

Theory and simulations predict that the structural concert of protein folding reactions is
relatively low. Experimentally, folding cooperativity has been difficult to study, but in recent …

Weakly bound protein complexes play a crucial role in metabolic, regulatory, and signaling
pathways, due in part to the high tunability of their bound and unbound populations. This …

Established models of ternary complex formation between hormone, G protein coupled
receptor (GPCR), and G protein assume that all interactions occur under equilibrium …

The concomitant folding of a nascent protein domain with its synthesis can generate
mechanical forces that act on the ribosome and alter translation speed. Such changes in …

A question of fundamental importance concerning protein folding in vivo is whether the
kinetics of translation or the thermodynamics of the ribosome nascent chain (RNC) complex …

Differential scanning calorimetry (DSC) is a very powerful tool for investigating protein
folding and stability because its experimental output reflects the energetics of all …

The concomitant folding of a protein with its synthesis on the ribosome is influenced by a
number of different timescales including the translation rate. Here we present a kinetic …

It has been observed for several proteins that slowing down the rate at which individual
codons are translated can increase their probability of cotranslational protein folding, while …

Identifying and understanding the differences between protein folding in bulk solution and in
the cell is a crucial challenge facing biology. Using Langevin dynamics, we have simulated …