Ontology highlight
ABSTRACT:
SUBMITTER: Li C
PROVIDER: S-EPMC2645536 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Li Conggang C Pielak Gary J GJ
Journal of the American Chemical Society 20090201 4
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. ...[more]