Predicting the rotational tumbling of dynamic multidomain proteins and 
supramolecular complexes.

Rezaei-Ghaleh, N.; Klama, F.; Munari, F.; Zweckstetter, M.

doi:10.1002/anie.201305094

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Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes.

MPS-Authors

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Rezaei-Ghaleh, N.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Munari, F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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引用

Rezaei-Ghaleh, N., Klama, F., Munari, F., & Zweckstetter, M. (2013). Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes. Angewandte Chemie International Edition, 52(43), 11410-11414. doi:10.1002/anie.201305094.

引用: https://hdl.handle.net/11858/00-001M-0000-0015-87F4-5

要旨

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.