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Efficient Modeling of Symmetric Protein Aggregates from NMR Data
Author(s) -
Bardiaux Benjamin,
van Rossum BarthJan,
Nilges Michael,
Oschkinat Hartmut
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201783
Subject(s) - homogeneous space , dihedral angle , monomer , point (geometry) , symmetry (geometry) , computer science , dihedral group , information retrieval , combinatorics , crystallography , data mining , algorithm , chemistry , mathematics , physics , nuclear magnetic resonance , molecule , geometry , group (periodic table) , organic chemistry , hydrogen bond , polymer
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.