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Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

Fraga, Hugo , Arnaud, Charles-Adrien, Gauto, Diego F., Audin, Maxime, Kurauskas, Vilius, Macek, Pavel , Krichel, Carsten, Guan, Jia-Ying, Boisbouvier, Jerome , Sprangers, Remco, Breyton, Cécile and Schanda, Paul (2017) Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins. ChemPhysChem 18 (19), pp. 2697-2703.

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Other URL: http://doi.org/10.1002/cphc.201700572


Abstract

Solid-state NMR spectroscopy can provide insight into protein structure and dynamics at the atomic level without inherent protein size limitations. However, a major hurdle to studying large proteins by solid-state NMR spectroscopy is related to spectral complexity and resonance overlap, which increase with molecular weight and severely hamper the assignment process. Here the use of two sets of ...

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Item type:Article
Date:2017
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Identification Number:
ValueType
10.1002/cphc.201700572DOI
Keywords:PROTON-DETECTED NMR; ANGLE-SPINNING NMR; BACKBONE ASSIGNMENT; PERDEUTERATED PROTEINS; HIGH-RESOLUTION; ATOMIC MODEL; FAST MAS; 100 KHZ; SPECTROSCOPY; LINKING; NMR methods; NMR pulse sequences; phage proteins; protein assemblies; protein quality control machinery
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:39684
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