Efficient modeling of symmetric protein aggregates from NMR data.
An efficient approach to determine the structures of symmetric protein aggregates from liquid and solid-state NMR data is presented. Any symmetry can be used (cyclic or dihedral point symmetries, helical symmetries, crystallographic symmetries). Because the starting point is the random structure of the monomer, the knowledge of the 3D structure of the monomer is not required.
NMR Supported Structural Biology, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
Benjamin
B
Bardiaux
Barth-Jan
BJ
van Rossum
Michael
M
Nilges
Hartmut
H
Oschkinat
D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry*
D011506:Proteins