title: Intermolecular Paramagnetic Relaxation Enhancement (PRE) Studies of Transient Complexes in Intrinsically Disordered Proteins.
abstract: NMR interchain paramagnetic relaxation enhancement (PRE) techniques are a very powerful approach for detecting transient interchain interactions between intrinsically disordered proteins. These experiments, requiring a mixed sample containing a 1:1 ratio of isotope-labeled (15)N protein and natural abundance (14)N protein with a paramagnetic spin label, provide data that is limited to interchain interactions only. Application of these experiments to weakly associated transient species such as those that are present in the very early stages of self-assembly processes will aid our understanding of protein aggregation or fibril formation processes.
authors.affiliation: Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA.
authors.forename: Maria K
authors.initials: MK
authors.lastname: Janowska
authors.affiliation: Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ, 08854, USA. jean.baum@rutgers.edu.|Center for Integrative Proteomics Research, Rutgers University, 174 Frelinghuysen Road, Piscataway, NJ, 08854-8076, USA. jean.baum@rutgers.edu.
authors.forename: Jean
authors.initials: J
authors.lastname: Baum
mesh_terms: D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D007553:Isotope Labeling; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D066329:Protein Aggregates / Q000235:genetics; D011487:Protein Conformation; D013113:Spin Labels
chemical_list: D064267:Intrinsically Disordered Proteins; D066329:Protein Aggregates; D013113:Spin Labels
keywords: Aggregation; Intermolecular interactions; NMR; PRE; Paramagnetic relaxation enhancement