Use of stopped-flow fluorescence spectroscopy to measure rapid membrane binding by protein kinase C.

Abstract

AbstractIn investigating the binding of ligands to proteins, many studies have been concerned with answering the fundamental questions proposed by Scatchard (1), that is, “How many” and “How tightly bound?” Although these questions are of utmost importance, the kineticist also wishes to know “How rapidly?” The development of rapid kinetic methodologies has provided many of the tools to answer the latter question (2–4). Suitably designed kinetic experiments may, in many instances, be able to provide answers to the former questions as well. Moreover, kinetic studies may yield mechanistic insight that cannot be elucidated from other approaches.KeywordsFluorescence Resonance Energy TransferPhospholipid VesiclePlumbing LineObserve Rate ConstantVesicle ConcentrationThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.