Glassy dynamics of side-chain ordering in a simple model of protein folding.
We introduce a modified version of protein lattice models in which monomers have several spin states, representing side-chain rotamers. Completion of folding corresponds to reaching the native backbone configuration with complete ordering of side chains. We find that as temperature is lowered, side-chain ordering becomes much slower than backbone folding. The presence of side chains leads to nonexponential kinetics and a broad distribution of relaxation times.
Kussell
Edo
E
Department of Biophysics, Harvard University, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Shakhnovich
Eugene I
EI
D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins