期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 75, 期 3, 页码 569-585出版社
WILEY
DOI: 10.1002/prot.22268
关键词
NMR; ARIA; protein structure determination; NMR spectral assignment; network anchoring; symmetric homodimer calculation; spin-diffusion
资金
- Institut Pasteur
- CNRS
- FU Network Extend-NMR
- Action Incitative Concertee (ACI) IMPBio (ICMD_RMN)
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.
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