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Influence of different assignment conditions on the determination of symmetric homodimeric structures with ARIA
Author(s) -
Bardiaux Benjamin,
Bernard Aymeric,
Rieping Wolfgang,
Habeck Michael,
Malliavin Thérèse E.,
Nilges Michael
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22268
Subject(s) - anchoring , convergence (economics) , computer science , diffusion , spin (aerodynamics) , biological system , algorithm , mathematics , chemistry , physics , biology , engineering , quantum mechanics , structural engineering , thermodynamics , economics , economic growth
The ambiguous restraint for iterative assignment (ARIA) approach for NMR structure calculation is evaluated for symmetric homodimeric proteins by assessing the effect of several data analysis and assignment methods on the structure quality. In particular, we study the effects of network anchoring and spin‐diffusion correction. The spin‐diffusion correction improves the protein structure quality systematically, whereas network anchoring enhances the assignment efficiency by speeding up the convergence and coping with highly ambiguous data. For some homodimeric folds, network anchoring has been proved essential for unraveling both chain and proton assignment ambiguities. Proteins 2009. © 2008 Wiley‐Liss, Inc.