Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein
Autor: | Wiktor Koźmiński, Eliezer Masliah, Piotr Byrski, Robert Konrat, Michał Górka, Karin Ledolter, Szymon Żerko, Paweł Włodarczyk-Pruszyński |
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Jazyk: | angličtina |
Předmět: |
0301 basic medicine
Magnetic Resonance Spectroscopy Nonuniform sampling tau Proteins 010402 general chemistry Intrinsically disordered proteins 01 natural sciences Resonance (particle physics) Isotropic mixing Biochemistry Article 03 medical and health sciences MOCCA-XY16 High-dimensionality NMR Protein Isoforms Amino Acid Sequence Non-uniform sampling Nuclear Magnetic Resonance Biomolecular Mixing (physics) Spectroscopy Chemistry Distinctive feature Nuclear magnetic resonance spectroscopy 0104 chemical sciences Crystallography 030104 developmental biology Resonance assignment alpha-Synuclein Biological system |
Zdroj: | Journal of Biomolecular Nmr |
ISSN: | 0925-2738 |
DOI: | 10.1007/s10858-016-0048-7 |
Popis: | New experiments dedicated for large IDPs backbone resonance assignment are presented. The most distinctive feature of all described techniques is the employment of MOCCA-XY16 mixing sequences to obtain effective magnetization transfers between carbonyl carbon backbone nuclei. The proposed 4 and 5 dimensional experiments provide a high dispersion of obtained signals making them suitable for use in the case of large IDPs (application to 354 a. a. residues of Tau protein 3x isoform is presented) as well as provide both forward and backward connectivities. What is more, connecting short chains interrupted with proline residues is also possible. All the experiments employ non-uniform sampling. Electronic supplementary material The online version of this article (doi:10.1007/s10858-016-0048-7) contains supplementary material, which is available to authorized users. |
Databáze: | OpenAIRE |
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