Characterization of collective and anisotropic reorientational protein dynamics.
Intramolecular reorientational dynamics of proteins are described in terms of reorientational quasiharmonic modes. These modes provide important insight into anisotropic and collective axial fluctuations of distinct molecular fragments, and they represent a highly compact description of intramolecular protein motions that are spectroscopically observable via nuclear spin relaxation. The method is applied to a molecular dynamics computer simulation of the protein ubiquitin.
Lienin
S F
SF
Carlson School of Chemistry and Biochemistry, Clark University, Worcester, Massachusetts 01610, USA.
Brüschweiler
R
R
D016880:Anisotropy; D003198:Computer Simulation; D008962:Models, Theoretical; D009010:Monte Carlo Method; D011506:Proteins / Q000737:chemistry*; D014452:Ubiquitins / Q000737:chemistry
D011506:Proteins; D014452:Ubiquitins