Functional modes of proteins are among the most robust.
It is shown that a small subset of modes which are likely to be involved in protein functional motions of large amplitude can be determined by retaining the most robust normal modes obtained using different protein models. This result should prove helpful in the context of several applications proposed recently, like for solving difficult molecular replacement problems or for fitting atomic structures into low-resolution electron density maps. It may also pave the way for the development of methods allowing us to predict such motions accurately.
Nicolay
S
S
Laboratoire de Physique, Ecole Normale Supérieure, 46 allées d Italie, 69364 Lyon Cedex 07, France.
Sanejouand
Y-H
YH
D019295:Computational Biology; D003198:Computer Simulation; D003627:Data Interpretation, Statistical; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins