title: Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition.
abstract: Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four β-strands separated by up to 15 Å in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network.
authors.affiliation: Joint BSC-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona), Parc Científic de Barcelona, Baldiri Reixac 10, 08028 Barcelona, Spain.
authors.forename: R Bryn
authors.initials: RB
authors.lastname: Fenwick
authors.forename: Santi
authors.initials: S
authors.lastname: Esteban-Martín
authors.forename: Barbara
authors.initials: B
authors.lastname: Richter
authors.forename: Donghan
authors.initials: D
authors.lastname: Lee
authors.forename: Korvin F A
authors.initials: KF
authors.lastname: Walter
authors.forename: Dragomir
authors.initials: D
authors.lastname: Milovanovic
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Nils A
authors.initials: NA
authors.lastname: Lakomek
authors.forename: Christian
authors.initials: C
authors.lastname: Griesinger
authors.forename: Xavier
authors.initials: X
authors.lastname: Salvatella
mesh_terms: D006860:Hydrogen Bonding; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D025801:Ubiquitin