Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions.
Conventional NMR approaches to detect weak protein binding and aggregation are hindered by the increased viscosity brought about by crowding. We describe a simple and reliable NMR method to distinguish viscosity effects from binding and aggregation under crowded conditions.
Li
Conggang
C
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Pielak
Gary J
GJ
D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D014783:Viscosity
D012710:Serum Albumin, Bovine