FEBS Letters · 2014 · 18 citations · 37 references
Life SciencesBiochemistryBiophysicsMolecular BiophysicsProtein-protein InteractionsRedox BiochemistryMagnetic Resonance SpectroscopyProtein Complex AnalysisProtein Complex DynamicsProtein DynamicsProtein StructureRelaxation MechanismsCytochrome C BindingElectron Paramagnetic Resonance RelaxationEncounter ComplexesNuclear Magnetic Resonance RelaxationNuclear Magnetic Resonance RelaxometryParamagnetic Relaxation EnhancementSpin ProbesStatistical Ensembles
Formation of an encounter complex is important for efficient protein complex formation. The encounter state consists of an ensemble of orientations of two proteins in the complex. Experimental description of such ensembles inherently suffers from insufficient data availability. We have measured paramagnetic relaxation enhancements (PRE) on cytochrome c peroxidase (CcP) caused by its partner cytochrome c (Cc) carrying a spin label. The data complement earlier PRE data of spin labelled CcP, identifying several new interactions. This work demonstrates the need of obtaining as many independent data sets as possible to achieve the most accurate description of an encounter complex.
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