Correction to: An automated iterative approach for protein structure refinement using pseudocontact shifts
| Autor: | Stefano Cucuzza, Oliver Zerbe, Peter Güntert, Andreas Plückthun |
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| Přispěvatelé: | University of Zurich, Zerbe, Oliver |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy 1303 Biochemistry Chemistry Protein Conformation Correction Proteins 1607 Spectroscopy 610 Medicine & health Biochemistry Protein structure 10019 Department of Biochemistry 570 Life sciences biology Biological system Nuclear Magnetic Resonance Biomolecular Spectroscopy |
| Zdroj: | J Biomol NMR |
| DOI: | 10.5167/uzh-210330 |
| Popis: | NMR structure calculation using NOE-derived distance restraints requires a considerable number of assignments of both backbone and sidechains resonances, often difficult or impossible to get for large or complex proteins. Pseudocontact shifts (PCSs) also play a well-established role in NMR protein structure calculation, usually to augment existing structural, mostly NOE-derived, information. Existing refinement protocols using PCSs usually either require a sizeable number of sidechain assignments or are complemented by other experimental restraints. Here, we present an automated iterative procedure to perform backbone protein structure refinements requiring only a limited amount of backbone amide PCSs. Already known structural features from a starting homology model, in this case modules of repeat proteins, are framed into a scaffold that is subsequently refined by experimental PCSs. The method produces reliable indicators that can be monitored to judge about the performance. We applied it to a system in which sidechain assignments are hardly possible, designed Armadillo repeat proteins (dArmRPs), and we calculated the solution NMR structure of YM |
| Databáze: | OpenAIRE |
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