Designable structures are easy to unfold.
We study the structural stability of models of proteins for which the selected folds are unusually stable to mutation, that is, designable. A two-dimensional hydrophobic-polar lattice model was used to determine designable folds and these folds were investigated through Langevin dynamics. We find that the phase diagram of these proteins depends on their designability. In particular, highly designable folds are found to be weaker, i.e., easier to unfold, than low designable ones. We expect this to be related to protein flexibility.
Dias
Cristiano L
CL
Physics Department, Rutherford Building, McGill University, 3600 rue University, Montréal, Québec H3A 2T8, Canada.
Grant
Martin
M
D000595:Amino Acid Sequence; D003198:Computer Simulation; D015195:Drug Design; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
D011506:Proteins