Analysis of correlated motion in antibody combining sites from molecular dynamics simulations.
The crystal structures of the NC6.8-antisweet taste ligand complex and the uncomplexed antibody structures display significant differences in the conformations of residues in the combining site. A molecular dynamics method was employed to understand the flexibility and correlated motion of key combining site residues in the uncomplexed antibody. The simulations reveal that residues that show conformational differences between the complex and uncomplexed structures display strong dynamical correlations. Extensive analysis of the dynamics trajectory using time correlation methods is presented.
Viswanathan
M
M
Center for Biophysics and Computational Biology, University of Illinois, Urbana, Illinois 61801, USA.
Linthicum
D S
DS
Subramaniam
S
S
D000085:Acetates / Q000737:chemistry*; D000911:Antibodies, Monoclonal / Q000737:chemistry*; D001666:Binding Sites, Antibody; D018360:Crystallography, X-Ray; D006146:Guanidines / Q000737:chemistry*; D011487:Protein Conformation; D013549:Sweetening Agents / Q000737:chemistry*
D000085:Acetates; D000911:Antibodies, Monoclonal; D006146:Guanidines; D013549:Sweetening Agents; C083643:NC 174