title: An ensemble of rapidly interconverting orientations in electrostatic protein-peptide complexes characterized by NMR spectroscopy.
abstract: Protein complex formation involves an encounter state in which the proteins are associated in a nonspecific manner and often stabilized by interactions between charged surface patches. Such patches are thought to bind in many different orientations with similar affinity. To obtain experimental evidence for the dynamics in encounter complexes, a model was created using the electron transfer protein plastocyanin and short charged peptides. Three plastocyanins with distinct surface charge distributions were studied. The experimental results from chemical shift perturbations, paramagnetic relaxation enhancement (PRE) NMR, and theoretical results from Monte Carlo simulations indicate the presence of multiple binding orientations that interconvert quickly and are dominated by long-range charge interactions. The PRE data also suggest the presence of highly transient orientations stabilized by short-range interactions.
authors: Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, 2333 CC Leiden (The Netherlands).
authors: Jia-Ying
authors: JY
authors: Guan
authors: Johannes M
authors: JM
authors: Foerster
authors: Jan W
authors: JW
authors: Drijfhout
authors: Monika
authors: M
authors: Timmer
authors: Anneloes
authors: A
authors: Blok
authors: G Matthias
authors: GM
authors: Ullmann
authors: Marcellus
authors: M
authors: Ubbink
mesh_terms: D008958:Models, Molecular; D009010:Monte Carlo Method; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D055672:Static Electricity
chemical_list: D010455:Peptides; D011506:Proteins
keywords: NMR spectroscopy; encounter complexes; molecular modeling; plastocyanins; tetralysine peptides