Trimethylamine -oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine.

We report experimental and computational studies investigating the effects of three osmolytes, trimethylamine -oxide (TMAO), betaine, and glycine, on the hydrophobic collapse of an elastin-like polypeptide (ELP). All three osmolytes stabilize collapsed conformations of the ELP and reduce the lower critical solution temperature (LSCT) linearly with osmolyte concentration. As expected from conventional preferential solvation arguments, betaine and glycine both increase the surface tension at the air-water interface.

Overdamped dynamics of folded protein domains within a locally harmonic basin using coarse graining based on a partition of compact flexible clusters.

A coarse-graining method based on the partitioning of atoms into compact flexible clusters is used to formulate the dynamics of the nonequilibrium response of a protein to ligand dissociation. The α-carbon positions are used as the degrees of freedom. The net stiffness between each pair of neighboring α-carbons is calculated for the quasi-static, overdamped regime within the harmonic (quadratic potential energy surface) using the equivalent stiffness matrix of the network of atoms occupying the intervening space within the locally interacting region.

Response of rotation-translation blocked proteins using Langevin dynamics on a locally harmonic landscape.

Langevin dynamics is used to compute the time evolution of the nonequilibrium motion of the atomic coordinates of a protein in response to ligand dissociation. The protein potential energy surface (PES) is approximated by a harmonic basin about the minimum of the unliganded state. Upon ligand dissociation, the protein undergoes relaxation from the bound to the unbound state.