Efficient modeling of symmetric protein aggregates from NMR data

Lien vers Pubmed [PMID] – 22653848

Angew. Chem. Int. Ed. Engl. 2012 Jul;51(28):6916-9

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.