title: Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes.
abstract: 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.
authors.affiliation: Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Am Fassberg 11, 37077 Göttingen (Germany); Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany). nare@nmr.mpibpc.mpg.de.
authors.forename: Nasrollah
authors.initials: N
authors.lastname: Rezaei-Ghaleh
authors.forename: Frederik
authors.initials: F
authors.lastname: Klama
authors.forename: Francesca
authors.initials: F
authors.lastname: Munari
authors.forename: Markus
authors.initials: M
authors.lastname: Zweckstetter
mesh_terms: D057446:Hydrodynamics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins
keywords: NMR spectroscopy; hydrodynamic coupling; protein disorder; proteins; rotational diffusion