Probing transient conformational states of proteins by solid-state R 1ρ relaxation-dispersion NMR spectroscopy

Angewandte Chemie - International Edition

Volumn 53, Issue 17, 2014, Pages 4312-4317

  Ma, Peixiang ^a,b   Haller, Jens D ^a,b   Zajakala, Jérémy ^a,b   Macek, Pavel ^a,b   Sivertsen, Astrid C ^a,b   Willbold, Dieter ^a,b,c,d   Boisbouvier, Jérôme ^a,b   Schanda, Paul ^a,b  

^a UNIV GRENOBLE ALPES   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c HEINRICH HEINE UNIVERSITY   (Germany)

^d FORSCHUNGSZENTRUM JÜLICH   (Germany)

Author keywords

protein dynamics; relaxation dispersion; solid state NMR spectroscopy; transient conformations; ubiquitin

Indexed keywords

DISPERSIONS; EXPERIMENTS; MAGIC ANGLE SPINNING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID STATE PHYSICS;

BIOMOLECULAR REACTIONS; CONFORMATIONAL STATE; PROTEIN DYNAMICS; RELAXATION DISPERSION; SOLID-STATE NMR SPECTROSCOPY; STRUCTURAL FEATURE; THERMODYNAMICS AND KINETICS; UBIQUITIN;

PROTEINS;

DEUTERIUM; PROTEIN; PROTON; UBIQUITIN;

CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; NUCLEAR MAGNETIC RESONANCE; PROCEDURES; PROTEIN CONFORMATION; THERMODYNAMICS;

DEUTERIUM; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEINS; PROTONS; THERMODYNAMICS; UBIQUITIN;

EID: 84898965855     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201311275     Document Type: Article

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