Predicting the Rotational Tumbling of Dynamic Multidomain Proteins and Supramolecular Complexes

Predicting the Rotational Tumbling of Dynamic Multidomain Proteins and Supramolecular Complexes

Time is of the essence: The rotational motion of biomolecules depends on intra‐ and intermolecular interactions and thus on distinct functional states. A new method, called HYCUD accurately predicts rotational correlation times in complex dynamic systems. It gives insights into the motional behavior...

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Veröffentlicht in:Angewandte Chemie International Edition 2013-10, Vol.52 (43), p.11410-11414
Hauptverfasser: Rezaei-Ghaleh, Nasrollah, Klama, Frederik, Munari, Francesca, Zweckstetter, Markus
Format: Artikel
Sprache:eng
Schlagworte:
Biomolecules
Correlation
Dynamical systems
Dynamics
hydrodynamic coupling
Hydrodynamics
Magnetic Resonance Spectroscopy
Models, Molecular
Motional
NMR spectroscopy
Protein Conformation
protein disorder
Proteins
Proteins - chemistry
Rotational
rotational diffusion
Tumbling
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Beschreibung
Zusammenfassung:Time is of the essence: The rotational motion of biomolecules depends on intra‐ and intermolecular interactions and thus on distinct functional states. A new method, called HYCUD accurately predicts rotational correlation times in complex dynamic systems. It gives insights into the motional behavior of multidomain proteins in their free form and in supramolecular complexes.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201305094